Kenneth Williams, PhD
Research & Publications
Biography
News
Research Summary
Most of Dr. Williams’ career has been devoted to bringing state-of-the-art genomics, proteomics, biophysics, and high performance computing (HPC) technologies within reach of Yale and as many non-Yale investigators as possible. To pursue this goal more fully and to support the biotechnology research needed to provide cutting edge technologies, in 2000 Dr. Williams began submitting biotechnology Center grants instead of trying to renew the NIH and NSF grants that had supported his structure/function research program on single-strand RNA and DNA binding proteins and that, as described in the Introduction in Stone et al [(2007) Yale J. Biol Med. 80(4):195-211 (PMCID: PMC2347368)], also had provided the impetus for Dr. Williams to found the Keck Laboratory in 1980.
Upon being named by YSM on 7/1/2014 as “Founder” of the Keck Laboratory, Dr. Williams’ responsibilities were changed from serving as the Co-Director of the Keck Laboratory to his current focus on finding new applications for Parallel Reaction Monitoring (PRM) and other key mass spectrometry technologies available from the Keck Laboratory and on helping Yale investigators to obtain the grant funding needed to bring these technologies to bear on biomedical research. To implement this new direction Dr. Williams has focused on three areas of research with the first being to continue his >28 year collaboration with Dr. Angus Nairn that is directed at identifying the adaptive changes in neuronal protein signaling that occur in response to substances of abuse. This research, which is funded through at least 2020 with a P30 Center Grant, is carried out in the Yale/NIDA Neuroproteomics Center that was founded by Dr. Williams in 2005 and that since 2015 has been Co-Directed by Drs. Williams and Nairn. To implement a second area of research Dr. Williams collaborated with Drs. Chirag Parikh and Lloyd Cantley to develop a Targeted Urine Proteome Assay (TUPA) that was then used to identify protein biomarkers of delayed recovery after kidney transplant. This research is described in Cantley et al [(2016) Proteomics Clinical Applications 10, 58-74 (PMCID: PMC5003777)] and Williams et al [(2017) Proteomics Clinical Applications 11, 7-8 (PMID: 28261998)] and also in a provisional patent application, “Compositions and Methods for Identifying Protein Biomarkers of Delayed Recovery After Kidney Transplant”. The goal of this research is to develop a clinically useful assay for early prediction of Delayed Graft Function (DGF) that would improve treatment for patients at highest risk of DGF and that could offer insights into novel therapeutic strategies. Finally, a Brozeman Foundation Pilot Project Grant enabled a collaboration to be initiated with Drs. TuKiet Lam, Gil Mor, Navin Rauniyar, and Hongyu Zhao to implement a third area of research that is directed at identifying serum protein biomarkers to enable the early detection of ovarian cancer. As described in Rauniyar et al [(2017) Biomarkers Insight 12, 1-12 (PMCID: PMC5462478)] and also in a provisional patent application (“Targeted Ovarian Cancer Proteome Assay (TOCPA) for Early Detection of Ovarian Cancer”, Application No. 62/499,939 filed February 8, 2017), a Data Independent Acquisition (DIA)/Parallel Reaction Monitoring (PRM) workflow was implemented to identify improved serum protein biomarkers for ovarian cancer.
Investigators who would like assistance writing the grant applications that are needed to bring mass spectrometry to bear on their proteomics research are encouraged to contact kenneth.williams@yale.edu.
Extensive Research Description
A major focus of Dr. Williams is overseeing and continuously improving the Yale/NIDA Neuroproteomics Center that brings exceptionally strong Yale programs in proteomics and signal transduction in the brain together with neuroscientists from nine other institutions across the U.S. to identify adaptive changes in protein signaling that occur in response to substances of abuse. Twenty-three faculty with established records of highly innovative research into the molecular actions of psychoactive addictive drugs, as well as of other basic aspects of neurobiology, are working together in a unique synergy with the Keck Foundation Biotechnology Laboratory to support the Yale/NIDA Neuroproteomics Center. The main goal of the Center, whose theme is “Proteomics of Altered Signaling in Addiction”, is to use cutting edge proteomic technologies to analyze neuronal signal transduction mechanisms and the adaptive changes in these processes that occur in response to drugs of abuse. With Co-Directors Drs. Angus Nairn (Psychiatry) and Kenneth Williams (Mol. Biophys. & Biochem.) in the Administration Core, the Center includes Discovery Proteomics (DPC) and Targeted Proteomics (TPC) Cores. Biophysical technologies from the DPC extend protein profiling analyses into the functional domain while lipid analyses from the DPC positively leverage proteome level analyses to provide an increasingly biological systems level approach. A Bioinformatics and Biostatistics Core, which includes high performance computing and the Yale Protein Expression Database, provides essential support that positively leverages the value of each of the proteomic technology cores. A Pilot Research Project Core is a cornerstone in the Center’s efforts to encourage strong mentoring relationships that help attract and train future outstanding scientists. Behavioral adaptations that accompany drug addiction are believed to result from both short and long-term adaptive changes in brain reward centers. Thus, exposure to drugs of abuse regulates intracellular signaling processes that alter gene expression, protein translation, and protein post-translational modifications. Repeated exposure to drugs of abuse leads to stable alterations in these signaling systems that are critical for the changes in brain chemistry and structure of the addicted brain. The Center’s research goals include analysis of the actions of cannabis, cocaine, nicotine, and opioids on these intracellular signaling pathways in brain reward areas and development of methods that enable proteomic analysis of the single types of neurons that define the circuits that underlie the actions and addictive properties of drugs of abuse. Targeted and data-independent mass spectrometry analyses of signaling proteins implicated in the actions of drugs of abuse are being used to analyze the impact of substance abuse on the neuroproteome with motif-based, “Top-Down” MS/MS, and other approaches being used to study protein post-translational modifications. A major initiative led by the Bioinformatics and Biostatistics Core is to develop novel methods for deep integration of genomic, transcriptomic, and proteomic data with brain region and cell type-specificity.
A second area of interest for Dr. Williams is identifying the early protein biomarkers of Delayed Graft Function (DGF) following kidney transplant that are needed to improve the treatment of patients at highest risk of DGF. Kidney function during the first week following renal transplant varies tremendously, with some recipients experiencing immediate graft function (IGF, characterized by a rapid fall in serum creatinine), while others exhibit DGF and require at least one treatment of dialysis post-transplant. While DGF occurs infrequently in living donor kidney transplants, its incidence in deceased donor transplants is 20 to 33%. Recent strategies for increasing the recipient (e.g., elderly) and donor pools have also increased the risk of sub-optimal allograft function. Hence, both “extended-criteria donor” (ECD) and “donation after circulatory determination of death” (DCD) kidneys are associated with higher rates of DGF as compared with standard-criteria kidneys. The short term negative impact of DGF, which is caused primarily by ischemia-reperfusion injury (IRI) during allograft procurement and transplantation, includes increased lengths of stay and hospital costs primarily because of the need for dialysis. Over the longer term, DGF is associated with a >40% increased risk of graft loss. Current approaches for diagnosing DGF or SGF often include need for dialysis, changes in serum creatinine, and urine output. However, all three approaches are retrospective and can be confounded by residual native kidney function. As with other forms of acute kidney injury (AKI) caused by IRI, the delay in diagnosis necessitated by these retrospective approaches greatly impedes efforts to prevent or treat renal injury. Such a delay is particularly pernicious in the setting of transplant as the most common immunosuppression regimens utilize nephrotoxic calcineurin inhibitors. Rapidly distinguishing DGF from IGF post-operatively could allow early tailoring of immunosuppressants, both agents and doses, to renal function. Current research centers on the use of the Targeted Urine Proteome Assay (TUPA) that was described by Cantley et al [(2016) Proteomics Clinical Applications 10, 58-74 (PMCID: PMC5003777)] to identify protein biomarkers of delayed recovery from kidney transplant. Potential biomarkers were identified by using the TUPA Multiple Reaction Monitoring (MRM) assay to interrogate the relative DGF/IGF levels of expression of 167 proteins in urine taken 12-18 hours after kidney implantation from 21 DGF, 15 SGF (slow graft function), and 16 IGF patients. An iterative Random Forest analysis approach evaluated the relative importance of each biomarker, which was then used to identify an optimum biomarker panel that provided the maximum sensitivity and specificity with the least number of biomarkers. Four proteins (C4b-binding protein alpha, guanylin, immunoglobulin superfamily member 8, and serum amyloid P-component) were identified that together distinguished DGF with a sensitivity of 82.6%, specificity of 77.4% and AUC of 0.891. This panel represents an important step towards identifying DGF at an early stage so that more effective treatments can be developed to improve long term graft outcomes. Future studies will be directed at validating these results in an independent patient cohort and at further improving this panel.
The third area of interest for Dr. Williams is identifying serum protein biomarkers for ovarian cancer. With an incidence of 12.1 and death rate of 7.7 per 100000, ovarian cancer is the deadliest gynecological cancer and the fourth most frequent cause of cancer death in women. Ovarian cancer has been termed the “silent killer” because of the lack of early warning symptoms. Although ~90% of patients have symptoms (e.g. frequent urination, pelvic pain, fatigue, abdominal distension) before diagnosis; the symptoms usually are too vague to prompt a visit to a physician or are easily confused with other illnesses. Hence, ~70% of women diagnosed with this cancer have advanced disease, where the 5-year survival rates are <30%. In contrast, for the ~15% of patients who are diagnosed early when the cancer is confined to the primary site (i.e., Stage 1), the 5-year survival rate is >90%. The >3-fold increase in survival rates for patients with localized disease and the >14,000 deaths annually in the U.S. from ovarian cancer provide compelling justification for supporting the research needed to identify improved biomarkers for early stage detection. CA-125 and imaging are the most common approaches for ovarian cancer screening. However, these approaches, either alone or in combination, are not useful for routine screening due to their low specificity and/or sensitivity. For example, serum CA-125 has a sensitivity and specificity of only 69% and 84% respectively for detecting ovarian cancer. Due to the low prevalence of ovarian cancer, a useful screening strategy must have a sensitivity >80% for early-stage disease and specificity >99.6%. Our review of 36 published serum/plasma biomarker panels for ovarian cancer identified 11 panels that each used from 1-6 biomarkers to achieve >90% sensitivity and specificity [Rauniyar et al (2017) Biomarkers Insight 12, 1-12 (PMCID: PMC5462478)]. Since most of these panels share few, if any biomarkers in common, we reason that inclusion of as many of the biomarkers in these, and other previously reported panels, in a single biomarker panel would leverage >40 years of research by providing an opportunity to more rigorously compare the relative efficacies of each of these biomarkers that are detectable by mass spectrometry in the non-fractionated serum that we believe is the best biological sample for these studies and for then choosing the best biomarker panel with the highest possible sensitivity and specificity. In addition to screening, there is also a critical need for improved biomarkers for diagnosis of ovarian cancer. It has been estimated that 5-10% of women in the U.S. will undergo surgery for a suspected ovarian neoplasm during their lifetime and that 13-21% of these patients have ovarian cancer. Since most adnexal masses are benign, it is important to identify preoperatively those patients who are at high risk of ovarian cancer and who will benefit from referral to a gynecologic oncologist to ensure the best possible care. Although ovarian cancer patients operated on by gynecologic oncologists have a 6- to 9-month median survival benefit, only about one third of women with ovarian cancer are referred to a gynecologic oncologist for primary surgery. To meet the need for improved diagnosis of high risk ovarian tumors, the FDA has approved three multivariate index assays. However, even the most recently approved assay, Overa, has a specificity of only 69%. To identify biomarkers that will allow earlier screening and improved diagnosis, a Data Independent Acquisition (DIA) and Parallel Reaction Monitoring (PRM) mass spectrometry workflow was implemented to determine differentially regulated proteins in ovarian cancer versus control sera and to validate these and other literature biomarkers. DIA identified Apolipoprotein A-IV, which had an ovarian cancer/control fold change of 0.52, as the most significantly differentially regulated protein (Rauniyar et al, 2017). PRM analyses of 10 biomarkers with the Targeted Ovarian Cancer Proteome Assay (TOCPA) and Random Forest (RF) analyses validated these results and showed that C-reactive protein, transferrin, and transthyretin are the next best biomarkers. Based on TOCPA analyses, ApoA-IV has a larger fold-change than determined by immunological assays and it is a more reliable biomarker than ApoA-I, which is in the Overa test for detecting ovarian cancer in pelvic masses. All samples were classified correctly using a breakpoint at ~54.4% of the mean level of ApoA-IV in the controls. This research suggests a way to improve the Overa test and it provides a PRM platform and RF approach together with four promising biomarkers to speed the development of a clinical test for diagnosing ovarian cancer.
Coauthors
Research Interests
Mass Spectrometry; Proteomics; Tandem Mass Spectrometry; Biomarkers, Pharmacological
Public Health Interests
Cancer; Substance Use, Addiction
Research Image
Reproducibility of Technical Replicates from TOCPA Analyses of Three Apo-A4 Peptides
Selected Publications
- Differential Effects of Cocaine and Morphine on the Diurnal Regulation of the Mouse Nucleus Accumbens ProteomeKetchesin K, Becker-Krail D, Xue X, Wilson R, Lam T, Williams K, Nairn A, Tseng G, Logan R. Differential Effects of Cocaine and Morphine on the Diurnal Regulation of the Mouse Nucleus Accumbens Proteome Journal Of Proteome Research 2023 PMID: 37311105, DOI: 10.1021/acs.jproteome.3c00126.
- Uncovering biology by single-cell proteomicsMansuri M, Williams K, Nairn A. Uncovering biology by single-cell proteomics Communications Biology 2023, 6: 381. PMID: 37031277, PMCID: PMC10082756, DOI: 10.1038/s42003-023-04635-2.
- Use of a Targeted Urine Proteome Assay (TUPA) to identify protein biomarkers of delayed recovery after kidney transplantWilliams KR, Colangelo CM, Hou L, Chung L, Belcher JM, Abbott T, Hall IE, Zhao H, Cantley LG, Parikh CR. Use of a Targeted Urine Proteome Assay (TUPA) to identify protein biomarkers of delayed recovery after kidney transplant Proteomics Clinical Applications 2017, 11: 1600132. PMID: 28261998, PMCID: PMC5549272, DOI: 10.1002/prca.201600132.
- Data-Independent Acquisition and Parallel Reaction Monitoring Mass Spectrometry Identification of Serum Biomarkers for Ovarian CancerRauniyar N, Peng G, Lam TT, Zhao H, Mor G, Williams KR. Data-Independent Acquisition and Parallel Reaction Monitoring Mass Spectrometry Identification of Serum Biomarkers for Ovarian Cancer Biomarker Insights 2017, 12: 1177271917710948. PMID: 28615921, PMCID: PMC5462478, DOI: 10.1177/1177271917710948.
- Development of a Targeted Urine Proteome Assay for kidney diseasesCantley LG, Colangelo CM, Stone KL, Chung L, Belcher J, Abbott T, Cantley JL, Williams KR, Parikh CR. Development of a Targeted Urine Proteome Assay for kidney diseases Proteomics Clinical Applications 2015, 10: 58-74. PMID: 26220717, PMCID: PMC5003777, DOI: 10.1002/prca.201500020.
- YPED: An Integrated Bioinformatics Suite and Database for Mass Spectrometry-based Proteomics ResearchColangelo CM, Shifman M, Cheung KH, Stone KL, Carriero NJ, Gulcicek EE, Lam TT, Wu T, Bjornson RD, Bruce C, Nairn AC, Rinehart J, Miller PL, Williams KR. YPED: An Integrated Bioinformatics Suite and Database for Mass Spectrometry-based Proteomics Research Genomics Proteomics & Bioinformatics 2015, 13: 25-35. PMID: 25712262, PMCID: PMC4411476, DOI: 10.1016/j.gpb.2014.11.002.
- Development of a highly automated and multiplexed targeted proteome pipeline and assay for 112 rat brain synaptic proteinsColangelo CM, Ivosev G, Chung L, Abbott T, Shifman M, Sakaue F, Cox D, Kitchen RR, Burton L, Tate SA, Gulcicek E, Bonner R, Rinehart J, Nairn AC, Williams KR. Development of a highly automated and multiplexed targeted proteome pipeline and assay for 112 rat brain synaptic proteins Proteomics 2015, 15: 1202-1214. PMID: 25476245, PMCID: PMC4698340, DOI: 10.1002/pmic.201400353.
- Quantitative proteomics identification of potential protein biomarkers of early recovery after kidney transplant (591.5)Williams K, Colangelo C, Stone K, Chung L, Abbott T, Belcher J, Marlier A, Cantley L, Parikh C. Quantitative proteomics identification of potential protein biomarkers of early recovery after kidney transplant (591.5) The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.591.5.
- Quantitative proteomicsGulcicek E, Williams K. Quantitative proteomics Methods 2013, 61: 183-185. DOI: 10.1016/j.ymeth.2013.06.016.
- Proteomics and the Analysis of Proteomic Data: 2013 Overview of Current Protein‐Profiling TechnologiesBruce C, Stone K, Gulcicek E, Williams K. Proteomics and the Analysis of Proteomic Data: 2013 Overview of Current Protein‐Profiling Technologies Current Protocols In Bioinformatics 2013, 41: 13.21.1-13.21.17. PMID: 23504934, PMCID: PMC3688054, DOI: 10.1002/0471250953.bi1321s41.
- Yale Center for Clinical Investigation: Leveraging Industry Partnerships and Research CoresSherwin R, Slayman C, Rockwell S, Herold K, Williams K, Carson R, Mane S, Seow H, Max J, Johnson T. Yale Center for Clinical Investigation: Leveraging Industry Partnerships and Research Cores Clinical And Translational Science 2012, 5: 435-436. PMID: 23253663, PMCID: PMC5350809, DOI: 10.1111/cts.12016.
- A molecular characterization of the choroid plexus and stress-induced gene regulationSathyanesan M, Girgenti MJ, Banasr M, Stone K, Bruce C, Guilchicek E, Wilczak-Havill K, Nairn A, Williams K, Sass S, Duman JG, Newton SS. A molecular characterization of the choroid plexus and stress-induced gene regulation Translational Psychiatry 2012, 2: e139-e139. PMID: 22781172, PMCID: PMC3410626, DOI: 10.1038/tp.2012.64.
- Reverse-Phase HPLC Separation of Enzymatic Digests of ProteinsStone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins 2009, 941-950. DOI: 10.1007/978-1-59745-198-7_102.
- Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide GelsStone K, Gulcicek E, Williams K. Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels 2009, 905-917. DOI: 10.1007/978-1-59745-198-7_99.
- The putative oncoprotein DEK, part of a chimera protein associated with acute myeloid leukaemia, is an autoantigen in juvenile rheumatoid arthritisSIERAKOWSKA H, WILLIAMS K, SZER I, SZER W. The putative oncoprotein DEK, part of a chimera protein associated with acute myeloid leukaemia, is an autoantigen in juvenile rheumatoid arthritis Clinical & Experimental Immunology 2008, 94: 435-439. PMID: 8252804, PMCID: PMC1534440, DOI: 10.1111/j.1365-2249.1993.tb08214.x.
- X!!Tandem, an Improved Method for Running X!Tandem in Parallel on Collections of Commodity ComputersBjornson RD, Carriero NJ, Colangelo C, Shifman M, Cheung KH, Miller PL, Williams K. X!!Tandem, an Improved Method for Running X!Tandem in Parallel on Collections of Commodity Computers Journal Of Proteome Research 2007, 7: 293-299. PMID: 17902638, PMCID: PMC3863625, DOI: 10.1021/pr0701198.
- Identification of Proteins Based on MS/MS Spectra and Location of Posttranslational ModificationsStone K, Crawford M, McMurray W, Williams N, Williams K. Identification of Proteins Based on MS/MS Spectra and Location of Posttranslational Modifications 2007, 386: 57-77. DOI: 10.1007/1-59745-430-3_2.
- MALDI-MS Data Analysis for Disease Biomarker DiscoveryYu W, Wu B, Liu J, Li X, Stone K, Williams K, Zhao H. MALDI-MS Data Analysis for Disease Biomarker Discovery 2006, 328: 199-216. DOI: 10.1385/1-59745-026-x:199.
- Isotope-Coded Affinity Tags for Protein QuantificationColangelo C, Williams K. Isotope-Coded Affinity Tags for Protein Quantification 2006, 328: 151-158. DOI: 10.1385/1-59745-026-x:151.
- Statistical Methods in ProteomicsYu W, Wu B, Huang T, Li X, Williams K, Zhao H. Statistical Methods in Proteomics 2006, 623-638. DOI: 10.1007/978-1-84628-288-1_34.
- Proteomics and the Analysis of Proteomic Data: An Overview of Current Protein‐Profiling TechnologiesGulcicek EE, Colangelo CM, McMurray W, Stone K, Williams K, Wu T, Zhao H, Spratt H, Kurosky A, Wu B. Proteomics and the Analysis of Proteomic Data: An Overview of Current Protein‐Profiling Technologies Current Protocols In Bioinformatics 2005, 10: 13.1.1-13.1.31. PMID: 18428746, PMCID: PMC3863626, DOI: 10.1002/0471250953.bi1301s10.
- A High Productivity/Low Maintenance Approach to High-performance Computation for Biomedicine: Four Case StudiesCarriero N, Osier MV, Cheung KH, Miller PL, Gerstein M, Zhao H, Wu B, Rifkin S, Chang J, Zhang H, White K, Williams K, Schultz M. A High Productivity/Low Maintenance Approach to High-performance Computation for Biomedicine: Four Case Studies Journal Of The American Medical Informatics Association 2004, 12: 90-98. PMID: 15492032, PMCID: PMC543832, DOI: 10.1197/jamia.m1571.
- Expression profiling reveals novel pathways in the transformation of Melanocytes to Melanomas.Hoek K, Rimm D, Williams K, Zhao H, Ariyan S, Lin A, Kluger H, Berger A, Cheng E, Trombetta E, Wu T, Halaban R, Niinobe M, Yoshikawa K, Hannigan G. Expression profiling reveals novel pathways in the transformation of Melanocytes to Melanomas. Pigment Cell & Melanoma Research 2004, 17: 430-430. DOI: 10.1111/j.1600-0749.2004.00175_12.x.
- Comparison of statistical methods for classification of ovarian cancer using mass spectrometry dataWu B, Abbott T, Fishman D, McMurray W, Mor G, Stone K, Ward D, Williams K, Zhao H. Comparison of statistical methods for classification of ovarian cancer using mass spectrometry data Bioinformatics 2003, 19: 1636-1643. PMID: 12967959, DOI: 10.1093/bioinformatics/btg210.
- Reverse-Phase HPLC Separation of Enzymatic Digests of ProteinsStone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins 2002, 0: 533-540. DOI: 10.1385/1-59259-169-8:533.
- Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide GelsStone K, Williams K. Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels 2002, 0: 511-521. DOI: 10.1385/1-59259-169-8:511.
- PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*Tang J, Frankel A, Cook R, Kim S, Paik W, Williams K, Clarke S, Herschman H. PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells* Journal Of Biological Chemistry 2000, 275: 7723-7730. PMID: 10713084, DOI: 10.1074/jbc.275.11.7723.
- Identification of the RNA Binding Domain of T4 RegA Protein by Structure-based Mutagenesis*Gordon J, Sengupta T, Phillips C, O'Malley S, Williams K, Spicer E. Identification of the RNA Binding Domain of T4 RegA Protein by Structure-based Mutagenesis* Journal Of Biological Chemistry 1999, 274: 32265-32273. PMID: 10542265, DOI: 10.1074/jbc.274.45.32265.
- Identification of Protein-ArginineN-Methyltransferase as 10-Formyltetrahydrofolate Dehydrogenase*Kim S, Park G, Joo W, Paik W, Cook R, Williams K. Identification of Protein-ArginineN-Methyltransferase as 10-Formyltetrahydrofolate Dehydrogenase* Journal Of Biological Chemistry 1998, 273: 27374-27382. PMID: 9765265, DOI: 10.1074/jbc.273.42.27374.
- Use of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresisStone K, Deangelis R, LoPresti M, Jones J, Papov V, Williams K. Use of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis Electrophoresis 1998, 19: 1046-1052. PMID: 9638951, DOI: 10.1002/elps.1150190620.
- Enzymatic cleavage and HPLC peptide mapping of proteinsWilliams K, Stone K. Enzymatic cleavage and HPLC peptide mapping of proteins Molecular Biotechnology 1997, 8: 155-167. PMID: 9406186, DOI: 10.1007/bf02752260.
- Identification of N G-Methylarginine Residues in Human Heterogeneous RNP Protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe Is a Preferred Recognition Motif †Kim S, Merrill B, Rajpurohit R, Kumar A, Stone K, Papov V, Schneiders J, Szer W, Wilson S, Paik W, Williams K. Identification of N G-Methylarginine Residues in Human Heterogeneous RNP Protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe Is a Preferred Recognition Motif † Biochemistry 1997, 36: 5185-5192. PMID: 9136880, DOI: 10.1021/bi9625509.
- Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolutionShamoo Y, Krueger U, Rice L, Williams K, Steitz T. Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution Nature Structural & Molecular Biology 1997, 4: 215-222. PMID: 9164463, DOI: 10.1038/nsb0397-215.
- hnRNP A1 Binds Promiscuously to Oligoribonucleotides: Utilization of Random and Homo-Oligonucleotides to Discriminate Sequence from Base-Specific BindingAbdul-Manan N, Williams K. hnRNP A1 Binds Promiscuously to Oligoribonucleotides: Utilization of Random and Homo-Oligonucleotides to Discriminate Sequence from Base-Specific Binding Nucleic Acids Research 1996, 24: 4063-4070. PMID: 8918813, PMCID: PMC146211, DOI: 10.1093/nar/24.20.4063.
- Purification and characterization of a recombinant hepatitis E protein vaccine candidate by liquid chromatography-mass spectrometryMcAtee C, Zhang Y, Yarbough P, Fuerst T, Stone K, Samander S, Williams K. Purification and characterization of a recombinant hepatitis E protein vaccine candidate by liquid chromatography-mass spectrometry Journal Of Chromatography B 1996, 685: 91-104. PMID: 8930757, DOI: 10.1016/0378-4347(96)00143-0.
- Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide GelsStone K, Williams K. Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels 1996, 415-425. DOI: 10.1007/978-1-60327-259-9_71.
- Matrix-Assisted Laser Desorption Ionization Mass Spectrometry as a Complement to Internal Protein SequencingWilliams K, Samandar S, Stone K, Saylor M, Rush J. Matrix-Assisted Laser Desorption Ionization Mass Spectrometry as a Complement to Internal Protein Sequencing 1996, 541-555. DOI: 10.1007/978-1-60327-259-9_91.
- Reverse-Phase HPLC Separation of Enzymatic Digests of ProteinsStone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins 1996, 427-434. DOI: 10.1007/978-1-60327-259-9_72.
- Origins of Binding Specificity of the A1 Heterogeneous Nuclear Ribonucleoprotein †Abdul-Manan N, O'Malley S, Williams K. Origins of Binding Specificity of the A1 Heterogeneous Nuclear Ribonucleoprotein † Biochemistry 1996, 35: 3545-3554. PMID: 8639505, DOI: 10.1021/bi952298p.
- Digestion of Proteins in Gels for Sequence AnalysisStone K, Williams K. Digestion of Proteins in Gels for Sequence Analysis Current Protocols In Protein Science 1995, 00: 11.3.1-11.3.13. DOI: 10.1002/0471140864.ps1103s00.
- Structural specificity of substrate for S-adenosylmethionine protein arginine N-methyltransferasesRawal N, Rajpurohit R, Lischwe M, Williams K, Paik W, Kim S. Structural specificity of substrate for S-adenosylmethionine protein arginine N-methyltransferases Biochimica Et Biophysica Acta 1995, 1248: 11-18. PMID: 7536038, DOI: 10.1016/0167-4838(94)00213-z.
- Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide MappingWilliams K, Stone K. Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping 1995, 40: 157-175. DOI: 10.1385/0-89603-301-5:157.
- Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide MappingWilliams K, Stone K. Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping 1995, 40: 157-175. PMID: 7633521, DOI: 10.1385/0-89603-301-5:157.
- Mutagenesis of the COOH-terminal Region of Bacteriophage T4 regA Protein (∗)O'Malley S, Sattar A, Williams K, Spicer E. Mutagenesis of the COOH-terminal Region of Bacteriophage T4 regA Protein (∗) Journal Of Biological Chemistry 1995, 270: 5107-5114. PMID: 7890619, DOI: 10.1074/jbc.270.10.5107.
- Multiple RNA binding domains (RBDs) just don't add upShamoo Y, Abdul-Manan N, Williams K. Multiple RNA binding domains (RBDs) just don't add up Nucleic Acids Research 1995, 23: 725-728. PMID: 7535921, PMCID: PMC306750, DOI: 10.1093/nar/23.5.725.
- In gel digestion of SDS PAGE-Separated proteins: Observations from internal sequencing of 25 proteinsWilliams K, Stone K. In gel digestion of SDS PAGE-Separated proteins: Observations from internal sequencing of 25 proteins 1995, 6: 143-152. DOI: 10.1016/s1080-8914(06)80020-7.
- Both RNA-binding domains in heterogenous nuclear ribonucleoprotein A1 contribute toward single-stranded-RNA binding.Shamoo Y, Abdul-Manan N, Patten A, Crawford J, Pellegrini M, Williams K. Both RNA-binding domains in heterogenous nuclear ribonucleoprotein A1 contribute toward single-stranded-RNA binding. Biochemistry 1994, 33: 8272-81. PMID: 7518244, DOI: 10.1021/bi00193a014.
- Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts.Amrute S, Abdul-Manan Z, Pandey V, Williams K, Modak M. Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts. Biochemistry 1994, 33: 8282-91. PMID: 7518245, DOI: 10.1021/bi00193a015.
- Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy.Garrett D, Lodi P, Shamoo Y, Williams K, Clore G, Gronenborn A. Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 1994, 33: 2852-8. PMID: 8130198, DOI: 10.1021/bi00176a015.
- Translational Repression by the Bacteriophage T4 Gene 32 Protein Involves Specific Recognition of an RNA Pseudoknot StructureShamoo Y, Tam A, Konigsberg W, Williams K. Translational Repression by the Bacteriophage T4 Gene 32 Protein Involves Specific Recognition of an RNA Pseudoknot Structure Journal Of Molecular Biology 1993, 232: 89-104. PMID: 8331672, DOI: 10.1006/jmbi.1993.1372.
- Synthesis and Use of an Internal Amino Acid Sequencing Standard PeptideElliott J, Stone K, Williams K. Synthesis and Use of an Internal Amino Acid Sequencing Standard Peptide Analytical Biochemistry 1993, 211: 94-101. PMID: 8323041, DOI: 10.1006/abio.1993.1238.
- 2 Enzymatic Digestion of Proteins and HPLC Peptide IsolationStone K, Williams K. 2 Enzymatic Digestion of Proteins and HPLC Peptide Isolation 1993, 43-69. DOI: 10.1016/b978-0-08-092461-8.50009-5.
- Identification of amino acid residues at the interface of a bacteriophage T4 regA protein-nucleic acid complex.Webster K, Keill S, Konigsberg W, Williams K, Spicer E. Identification of amino acid residues at the interface of a bacteriophage T4 regA protein-nucleic acid complex. Journal Of Biological Chemistry 1992, 267: 26097-26103. PMID: 1464621, DOI: 10.1016/s0021-9258(18)35722-3.
- Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif.Nadler S, Kapouch J, Elliott J, Williams K. Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif. Journal Of Biological Chemistry 1992, 267: 3750-3757. PMID: 1740426, DOI: 10.1016/s0021-9258(19)50589-0.
- Randomization of Amino Acid Sequence: An Important Control In Synthetic Peptide Analogue Studies of Nucleic Acid Binding DomainsNadler S, Kapouch J, Elliott J, Williams K. Randomization of Amino Acid Sequence: An Important Control In Synthetic Peptide Analogue Studies of Nucleic Acid Binding Domains 1992, 163-170. DOI: 10.1016/b978-0-12-058756-8.50023-7.
- Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogasterShuai K, Gupta C, Hawley R, Chase J, Stone K, Williams K. Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster Nucleic Acids Research 1992, 20: 1379-1385. PMID: 1313969, PMCID: PMC312186, DOI: 10.1093/nar/20.6.1379.
- Elution and Internal Amino Acid Sequencing of PVDF-Blotted ProteinsStone K, LoPresti M, Williams K, Mcnulty D, Crawford J, DeAngelis R. Elution and Internal Amino Acid Sequencing of PVDF-Blotted Proteins 1992, 23-34. DOI: 10.1016/b978-0-12-058756-8.50008-0.
- State‐of‐the‐art biomolecular core facilities: a comprehensive survey1Niece R, Beach C, Cook R, Hathaway G, Williams K. State‐of‐the‐art biomolecular core facilities: a comprehensive survey1 The FASEB Journal 1991, 5: 2756-2760. PMID: 1916100, DOI: 10.1096/fasebj.5.13.1916100.
- A retrovirus-like zinc domain is essential for translational repression of bacteriophage T4 gene 32Shamoo Y, Webster K, Williams K, Konigsberg W. A retrovirus-like zinc domain is essential for translational repression of bacteriophage T4 gene 32 Journal Of Biological Chemistry 1991, 266: 7967-7970. PMID: 2022625, DOI: 10.1016/s0021-9258(18)92923-6.
- Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions.Nadler S, Merrill B, Roberts W, Keating K, Lisbin M, Barnett S, Wilson S, Williams K. Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions. Biochemistry 1991, 30: 2968-76. PMID: 1848781, DOI: 10.1021/bi00225a034.
- Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmidsRuvolo P, Keating K, Williams K, Chase J. Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids Proteins Structure Function And Bioinformatics 1991, 9: 120-134. PMID: 2008432, DOI: 10.1002/prot.340090206.
- Amino Acid Analysis and Sequencing — What is State-of-the-Art?Niece R, Ericsson L, Fowler A, Smith A, Speicher D, Crabb J, Williams K. Amino Acid Analysis and Sequencing — What is State-of-the-Art? 1991, 133-141. DOI: 10.1007/978-3-0348-5678-2_12.
- [25] Identification of amino acid residues at interface of protein—Nucleic acid complexes by photochemical cross-linkingWilliams K, Konigsberg W. [25] Identification of amino acid residues at interface of protein—Nucleic acid complexes by photochemical cross-linking 1991, 208: 516-539. PMID: 1779846, DOI: 10.1016/0076-6879(91)08027-f.
- Mammalian heterogeneous nuclear ribonucleoprotein A1. Nucleic acid binding properties of the COOH-terminal domain.Kumar A, Casas-Finet J, Luneau C, Karpel R, Merrill B, Williams K, Wilson S. Mammalian heterogeneous nuclear ribonucleoprotein A1. Nucleic acid binding properties of the COOH-terminal domain. Journal Of Biological Chemistry 1990, 265: 17094-17100. PMID: 2145269, DOI: 10.1016/s0021-9258(17)44873-3.
- A novel function for zinc(II) in a nucleic acid-binding protein. Contribution of zinc(II) toward the cooperativity of bacteriophage T4 gene 32 protein binding.Nadler S, Roberts W, Shamoo Y, Williams K. A novel function for zinc(II) in a nucleic acid-binding protein. Contribution of zinc(II) toward the cooperativity of bacteriophage T4 gene 32 protein binding. Journal Of Biological Chemistry 1990, 265: 10389-10394. PMID: 2113053, DOI: 10.1016/s0021-9258(18)86958-7.
- Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding.Meyers M, Keating K, Roberts W, Williams K, Chase J, Horwitz M. Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding. Journal Of Biological Chemistry 1990, 265: 5875-5882. PMID: 2318838, DOI: 10.1016/s0021-9258(19)39444-x.
- Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain.Kumar A, Widen S, Williams K, Kedar P, Karpel R, Wilson S. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain. Journal Of Biological Chemistry 1990, 265: 2124-2131. PMID: 2404980, DOI: 10.1016/s0021-9258(19)39949-1.
- 15 Design, Characterization and Results of ABRF-89SEQ: A Test Sample For Evaluating Protein Sequencer Performance in Protein Microchemistry Core FacilitiesSpeicher D, Grant G, Niece R, Blacher R, Fowler A, Williams K. 15 Design, Characterization and Results of ABRF-89SEQ: A Test Sample For Evaluating Protein Sequencer Performance in Protein Microchemistry Core Facilities 1990, 159-166. DOI: 10.1016/b978-0-12-721955-4.50021-x.
- Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structureMuniyappa K, Williams K, Chase J, Radding C. Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structure Nucleic Acids Research 1990, 18: 3967-3973. PMID: 2374716, PMCID: PMC331100, DOI: 10.1093/nar/18.13.3967.
- [21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteinsStone K, Elliott J, Peterson G, McMurray W, Williams K. [21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins 1990, 193: 389-412. PMID: 2074828, DOI: 10.1016/0076-6879(90)93429-o.
- p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39.Roberts W, Pan T, Elliott J, Coleman J, Williams K. p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39. Biochemistry 1989, 28: 10043-7. PMID: 2695161, DOI: 10.1021/bi00452a024.
- ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine- innervated brain regions. I. Amino acid sequence of ARPP-21B from bovine caudate nucleusWilliams K, Hemmings H, LoPresti M, Greengard P. ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine- innervated brain regions. I. Amino acid sequence of ARPP-21B from bovine caudate nucleus Journal Of Neuroscience 1989, 9: 3631-3637. PMID: 2552036, PMCID: PMC6569913, DOI: 10.1523/jneurosci.09-10-03631.1989.
- Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions.Shamoo Y, Ghosaini L, Keating K, Williams K, Sturtevant J, Konigsberg W. Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions. Biochemistry 1989, 28: 7409-17. PMID: 2684276, DOI: 10.1021/bi00444a039.
- The 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP HydrolysisRush J, Lin T, Quinones M, Spicer E, Douglas I, Williams K, Konigsberg W. The 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP Hydrolysis Journal Of Biological Chemistry 1989, 264: 10943-10953. PMID: 2786875, DOI: 10.1016/s0021-9258(18)60410-7.
- Structure/Function Relationships in the Bacteriophage T4 Single-Stranded DNA-Binding ProteinShamoo Y, Keating K, Williams K, Konigsberg W. Structure/Function Relationships in the Bacteriophage T4 Single-Stranded DNA-Binding Protein 1989, 302-322. DOI: 10.1007/978-1-4612-3652-8_14.
- 10 A SYNTHETIC PEPTIDE FOR EVALUATING PROTEIN SEQUENCER AND AMINO ACID ANALYZER PERFORMANCE IN CORE FACILITIES: DESIGN AND RESULTSNiece R, Williams K, Wadsworth C, Elliott J, Stone K, McMurray W, Fowler A, Atherton D, Kutny R, Smith A. 10 A SYNTHETIC PEPTIDE FOR EVALUATING PROTEIN SEQUENCER AND AMINO ACID ANALYZER PERFORMANCE IN CORE FACILITIES: DESIGN AND RESULTS 1989, 89-101. DOI: 10.1016/b978-0-12-682001-0.50016-6.
- 55 STRUCTURE OF SYMPOSIUM TEST PEPTIDE-3Elliott J, Crawford M, Stone K, Kapouch J, Roberts W, Jacobsen E, LoPresti M, Williams K, De Angelis R, McMurray W, Meng C, Mann M, Fenn J. 55 STRUCTURE OF SYMPOSIUM TEST PEPTIDE-3 1989, 569-579. DOI: 10.1016/b978-0-12-682001-0.50066-x.
- 37 ENZYMATIC DIGESTION OF PROTEINS AND HPLC PEPTIDE ISOLATION IN THE SUB-NANOMOLE RANGEStone K, LoPresti M, Williams N, Crawford J, DeAngelis R, Williams K. 37 ENZYMATIC DIGESTION OF PROTEINS AND HPLC PEPTIDE ISOLATION IN THE SUB-NANOMOLE RANGE 1989, 377-391. DOI: 10.1016/b978-0-12-682001-0.50046-4.
- Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particlesMerrill B, Barnett S, LeStourgeon W, Williams K. Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles Nucleic Acids Research 1989, 17: 8441-8449. PMID: 2587210, PMCID: PMC335017, DOI: 10.1093/nar/17.21.8441.
- The size, operation, and technical capabilities of protein and nucleic acid core facilities1Williams K, Niece R, Atherton D, Fowler A, Kutny R, Smith A. The size, operation, and technical capabilities of protein and nucleic acid core facilities1 The FASEB Journal 1988, 2: 3124-3130. PMID: 3192042, DOI: 10.1096/fasebj.2.15.3192042.
- Thermal denaturation of T4 gene 32 protein: effects of zinc removal and substitution.Keating K, Ghosaini L, Giedroc D, Williams K, Coleman J, Sturtevant J. Thermal denaturation of T4 gene 32 protein: effects of zinc removal and substitution. Biochemistry 1988, 27: 5240-5. PMID: 3262371, DOI: 10.1021/bi00414a044.
- Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein.Merrill B, Stone K, Cobianchi F, Wilson S, Williams K. Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein. Journal Of Biological Chemistry 1988, 263: 3307-3313. PMID: 2830282, DOI: 10.1016/s0021-9258(18)69073-8.
- Photochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinkingShamoo Y, Williams K, Konigsberg W. Photochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinking Proteins Structure Function And Bioinformatics 1988, 4: 1-6. PMID: 3186689, DOI: 10.1002/prot.340040103.
- Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids.Cobianchi F, Karpel R, Williams K, Notario V, Wilson S. Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids. Journal Of Biological Chemistry 1988, 263: 1063-1071. PMID: 2447078, DOI: 10.1016/s0021-9258(19)35461-4.
- Synthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus.Roberts W, Elliott J, McMurray W, Williams K. Synthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus. Chemical Biology & Drug Design 1988, 1: 74-80. PMID: 2856555.
- Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking.Pandey V, Williams K, Stone K, Modak M. Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking. Biochemistry 1987, 26: 7744-8. PMID: 3322406, DOI: 10.1021/bi00398a031.
- The function of zinc in gene 32 protein from T4.Giedroc D, Keating K, Williams K, Coleman J. The function of zinc in gene 32 protein from T4. Biochemistry 1987, 26: 5251-9. PMID: 3314985, DOI: 10.1021/bi00391a007.
- Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA.Spicer E, Horton R, Bloem L, Bach R, Williams K, Guha A, Kraus J, Lin T, Nemerson Y, Konigsberg W. Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 5148-5152. PMID: 3037536, PMCID: PMC298811, DOI: 10.1073/pnas.84.15.5148.
- Ferrate oxidation of Escherichia coli DNA polymerase-I. Identification of a methionine residue that is essential for DNA binding.Basu A, Williams K, Modak M. Ferrate oxidation of Escherichia coli DNA polymerase-I. Identification of a methionine residue that is essential for DNA binding. Journal Of Biological Chemistry 1987, 262: 9601-9607. PMID: 3298259, DOI: 10.1016/s0021-9258(18)47976-8.
- Use of HPLC Comparative Peptide Mapping in Structure/Function StudiesWilliams K, Stone K, Fritz M, Merrill B, Konigsberg W, Pandolfo M, Valentini O, Riva S, Reddigari S, Patel G, Chase J. Use of HPLC Comparative Peptide Mapping in Structure/Function Studies 1987, 45-52. DOI: 10.1007/978-1-4613-1787-6_5.
- Amino acid sequence of UP1, an hnRNP‐derived single‐stranded nucleic acid binding protein from calf thymusMERRILL B, LOPRESTI M, STONE K, WILLIAMS K. Amino acid sequence of UP1, an hnRNP‐derived single‐stranded nucleic acid binding protein from calf thymus Chemical Biology & Drug Design 1987, 29: 21-39. PMID: 3032834, DOI: 10.1111/j.1399-3011.1987.tb02226.x.
- Cloning of T4 gene 32 and expression of the wild-type protein under lambda promoter PL regulation in Escherichia coli.Shamoo Y, Adari H, Konigsberg W, Williams K, Chase J. Cloning of T4 gene 32 and expression of the wild-type protein under lambda promoter PL regulation in Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8844-8848. PMID: 2947239, PMCID: PMC387029, DOI: 10.1073/pnas.83.23.8844.
- Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein.Giedroc D, Keating K, Williams K, Konigsberg W, Coleman J. Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8452-8456. PMID: 3490667, PMCID: PMC386948, DOI: 10.1073/pnas.83.22.8452.
- Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.Kraus J, Firgaira F, Novotný J, Kalousek F, Williams K, Williamson C, Ohura T, Rosenberg L. Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8049-8053. PMID: 3464942, PMCID: PMC386864, DOI: 10.1073/pnas.83.21.8049.
- Escherichia coli exonuclease VII. Cloning and sequencing of the gene encoding the large subunit (xseA).Chase J, Rabin B, Murphy J, Stone K, Williams K. Escherichia coli exonuclease VII. Cloning and sequencing of the gene encoding the large subunit (xseA). Journal Of Biological Chemistry 1986, 261: 14929-14935. PMID: 3021756, DOI: 10.1016/s0021-9258(18)66806-1.
- Zinc metalloproteins involved in replication and transcriptionGiedroc D, Keating K, Martin C, Williams K, Coleman J. Zinc metalloproteins involved in replication and transcription Journal Of Inorganic Biochemistry 1986, 28: 155-169. PMID: 3543219, DOI: 10.1016/0162-0134(86)80079-4.
- Mammalian single‐stranded DNA binding protein UP I is derived from the hnRNP core protein A1.Riva S, Morandi C, Tsoulfas P, Pandolfo M, Biamonti G, Merrill B, Williams K, Multhaup G, Beyreuther K, Werr H. Mammalian single‐stranded DNA binding protein UP I is derived from the hnRNP core protein A1. The EMBO Journal 1986, 5: 2267-2273. PMID: 3023065, PMCID: PMC1167110, DOI: 10.1002/j.1460-2075.1986.tb04494.x.
- Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins.Kumar A, Williams K, Szer W. Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins. Journal Of Biological Chemistry 1986, 261: 11266-11273. PMID: 3733753, DOI: 10.1016/s0021-9258(18)67378-8.
- 1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis.Prigodich R, Shamoo Y, Williams K, Chase J, Konigsberg W, Coleman J. 1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis. Biochemistry 1986, 25: 3666-72. PMID: 3013293, DOI: 10.1021/bi00360a029.
- Single-Stranded DNA Binding Proteins Required for DNA ReplicationChase J, Williams K. Single-Stranded DNA Binding Proteins Required for DNA Replication Annual Review Of Biochemistry 1986, 55: 103-136. PMID: 3527040, DOI: 10.1146/annurev.bi.55.070186.000535.
- Acidic lipids enhance cathepsin D cleavage of the myelin basic proteinWilliams K, Williams N, Konigsberg W, Yu R. Acidic lipids enhance cathepsin D cleavage of the myelin basic protein Journal Of Neuroscience Research 1986, 15: 137-145. PMID: 2421004, DOI: 10.1002/jnr.490150203.
- Protein chemistry‐nuclear magnetic resonance approach to mapping functional domains in single‐stranded DNA binding proteinsColeman J, Williams K, King G, Prigodich R, Shamoo Y, Konigsberg W. Protein chemistry‐nuclear magnetic resonance approach to mapping functional domains in single‐stranded DNA binding proteins Journal Of Cellular Biochemistry 1986, 32: 305-326. PMID: 3543031, DOI: 10.1002/jcb.240320407.
- High-performance liquid chromatographic peptide mapping and amino acid analysis in the sub-nanomole rangeStone K, Williams K. High-performance liquid chromatographic peptide mapping and amino acid analysis in the sub-nanomole range Journal Of Chromatography 1986, 359: 203-212. PMID: 3733927, DOI: 10.1016/0021-9673(86)80074-7.
- High pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus.Merrill B, LoPresti M, Stone K, Williams K. High pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus. Journal Of Biological Chemistry 1986, 261: 878-883. PMID: 3941105, DOI: 10.1016/s0021-9258(17)36178-1.
- Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma.Williams K, Stone K, LoPresti M, Merrill B, Planck S. Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 5666-5670. PMID: 2994041, PMCID: PMC390612, DOI: 10.1073/pnas.82.17.5666.
- Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5.Williams K, Reddigari S, Patel G. Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 5260-5264. PMID: 2991914, PMCID: PMC390547, DOI: 10.1073/pnas.82.16.5260.
- Cloning, nucleotide sequence, and overexpression of the bacteriophage T4 regA gene.Adari H, Rose K, Williams K, Konigsberg W, Lin T, Spicer E. Cloning, nucleotide sequence, and overexpression of the bacteriophage T4 regA gene. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 1901-1905. PMID: 3872458, PMCID: PMC397441, DOI: 10.1073/pnas.82.7.1901.
- A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sitesKraus J, Hodges P, Williamson C, Horwich A, Kalousek F, Williams K, Rosenberg L. A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites Nucleic Acids Research 1985, 13: 943-952. PMID: 3839075, PMCID: PMC341044, DOI: 10.1093/nar/13.3.943.
- Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of gene 44 and its protein product.Spicer E, Nossal N, Williams K. Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of gene 44 and its protein product. Journal Of Biological Chemistry 1984, 259: 15425-15432. PMID: 6096371, DOI: 10.1016/s0021-9258(17)42566-x.
- Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation.Williams K, Murphy J, Chase J. Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation. Journal Of Biological Chemistry 1984, 259: 11804-11811. PMID: 6384214, DOI: 10.1016/s0021-9258(20)71283-4.
- Photochemical cross-linking of the Escherichia coli single-stranded DNA-binding protein to oligodeoxynucleotides. Identification of phenylalanine 60 as the site of cross-linking.Merrill B, Williams K, Chase J, Konigsberg W. Photochemical cross-linking of the Escherichia coli single-stranded DNA-binding protein to oligodeoxynucleotides. Identification of phenylalanine 60 as the site of cross-linking. Journal Of Biological Chemistry 1984, 259: 10850-10856. PMID: 6540775, DOI: 10.1016/s0021-9258(18)90591-0.
- Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine TranscarbamylaseHorwich A, Fenton W, Williams K, Kalousek F, Kraus J, Doolittle R, Konigsberg W, Rosenberg L. Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase Science 1984, 224: 1068-1074. PMID: 6372096, DOI: 10.1126/science.6372096.
- 1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes.Prigodich R, Casas-Finet J, Williams K, Konigsberg W, Coleman J. 1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes. Biochemistry 1984, 23: 522-9. PMID: 6367821, DOI: 10.1021/bi00298a019.
- A Rat Liver Helix-Destabilizing Protein: Properties and Homology to LDH-5Patel G, Reddigari S, Williams K, Baptist E, Thompson P, Sisodia S. A Rat Liver Helix-Destabilizing Protein: Properties and Homology to LDH-5 1984, 41-58. DOI: 10.1007/978-1-4612-5178-1_3.
- Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies.Chase J, L'Italien J, Murphy J, Spicer E, Williams K. Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies. Journal Of Biological Chemistry 1984, 259: 805-814. PMID: 6363409, DOI: 10.1016/s0021-9258(17)43529-0.
- F sex factor encodes a single-stranded DNA binding protein (SSB) with extensive sequence homology to Escherichia coli SSB.Chase J, Merrill B, Williams K. F sex factor encodes a single-stranded DNA binding protein (SSB) with extensive sequence homology to Escherichia coli SSB. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 5480-5484. PMID: 6351061, PMCID: PMC384281, DOI: 10.1073/pnas.80.18.5480.
- Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase.Horwich A, Kraus J, Williams K, Kalousek F, Konigsberg W, Rosenberg L. Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 4258-4262. PMID: 6576335, PMCID: PMC384016, DOI: 10.1073/pnas.80.14.4258.
- Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins.Williams K, Spicer E, LoPresti M, Guggenheimer R, Chase J. Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins. Journal Of Biological Chemistry 1983, 258: 3346-3355. PMID: 6298232, DOI: 10.1016/s0021-9258(18)32867-9.
- Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4McKay D, Williams K. Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4 Journal Of Molecular Biology 1982, 160: 659-661. PMID: 7175942, DOI: 10.1016/0022-2836(82)90321-7.
- Bacteriophage T4 gene 45. Sequences of the structural gene and its protein product.Spicer E, Noble J, Nossal N, Konigsberg W, Williams K. Bacteriophage T4 gene 45. Sequences of the structural gene and its protein product. Journal Of Biological Chemistry 1982, 257: 8972-8979. PMID: 6284751, DOI: 10.1016/s0021-9258(18)34228-5.
- Comparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive MutantsWilliams K, L’Italien J, Guggenheimer R, Sillerud L, Spicer E, Chase J, Konigsberg W. Comparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive Mutants 1982, 499-507. DOI: 10.1007/978-1-4612-5832-2_44.
- Primary structure of the bacteriophage T4 DNA helix-destabilizing protein.Williams K, LoPresti M, Setoguchi M. Primary structure of the bacteriophage T4 DNA helix-destabilizing protein. Journal Of Biological Chemistry 1981, 256: 1754-1762. PMID: 6257686, DOI: 10.1016/s0021-9258(19)69872-8.
- DNA helix-destabilizing proteins.Williams K, Konigsberg W. DNA helix-destabilizing proteins. Gene Amplification And Analysis 1981, 2: 475-508. PMID: 6765652.
- Amino acid sequence of the T4 DNA helix-destabilizing protein.Williams K, LoPresti M, Setoguchi M, Konigsberg W. Amino acid sequence of the T4 DNA helix-destabilizing protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 4614-4617. PMID: 6254033, PMCID: PMC349895, DOI: 10.1073/pnas.77.8.4614.
- DNA binding properties of the T4 DNA helix-destabilizing protein. A calorimetric study.Williams K, Sillerud L, Schafer D, Konigsberg W. DNA binding properties of the T4 DNA helix-destabilizing protein. A calorimetric study. Journal Of Biological Chemistry 1979, 254: 6426-6432. PMID: 221498, DOI: 10.1016/s0021-9258(18)50384-7.
- T4 gene 32 protein trypsin-generated fragments. Fluorescence measurement of DNA-binding parameters.Spicer E, Williams K, Konigsberg W. T4 gene 32 protein trypsin-generated fragments. Fluorescence measurement of DNA-binding parameters. Journal Of Biological Chemistry 1979, 254: 6433-6436. PMID: 221499, DOI: 10.1016/s0021-9258(18)50385-9.
- Structural characteristics of interferons from mouse Ehrlich ascites tumor cells.Cabrer B, Taira H, Broeze R, Kempe T, Williams K, Slattery E, Konigsberg W, Lengyel P. Structural characteristics of interferons from mouse Ehrlich ascites tumor cells. Journal Of Biological Chemistry 1979, 254: 3681-3684. PMID: 438151, DOI: 10.1016/s0021-9258(18)50635-9.
- Structural changes in the T4 gene 32 protein induced by DNA polynucleotides.Williams K, Konigsberg W. Structural changes in the T4 gene 32 protein induced by DNA polynucleotides. Journal Of Biological Chemistry 1978, 253: 2463-2470. PMID: 632279, DOI: 10.1016/s0021-9258(17)38096-1.
- Kinetic mechanism of tRNA nucleotidyltransferase from Escherichia coli.Williams K, Schofield P. Kinetic mechanism of tRNA nucleotidyltransferase from Escherichia coli. Journal Of Biological Chemistry 1977, 252: 5589-5597. PMID: 18468, DOI: 10.1016/s0021-9258(19)63391-0.
- Purification and some properties of Escherichia coli tRNA nucleotidyltransferase.Schofield P, Williams K. Purification and some properties of Escherichia coli tRNA nucleotidyltransferase. Journal Of Biological Chemistry 1977, 252: 5584-5588. PMID: 328503, DOI: 10.1016/s0021-9258(19)63390-9.
- Evidence for metalloenzyme character of tRNA nucleotidyl transferaseWilliams K, Schofield P. Evidence for metalloenzyme character of tRNA nucleotidyl transferase Biochemical And Biophysical Research Communications 1975, 64: 262-267. PMID: 238508, DOI: 10.1016/0006-291x(75)90247-8.