Kirill Grushin
Research Scientist in Cell Biology
Research & Publications
Biography
Coauthors
Selected Publications
- Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesiclesLi F, Grushin K, Coleman J, Pincet F, Rothman J. Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2306086120. PMID: 37883433, PMCID: PMC10623011, DOI: 10.1073/pnas.2306086120.
- Turbocharging synaptic transmissionRothman J, Grushin K, Bera M, Pincet F. Turbocharging synaptic transmission. FEBS Letters 2023, 597: 2233-2249. PMID: 37643878, DOI: 10.1002/1873-3468.14718.
- Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinerySundaram R, Chatterjee A, Bera M, Grushin K, Panda A, Li F, Coleman J, Lee S, Ramakrishnan S, Ernst A, Gupta K, Rothman J, Krishnakumar S. Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2309516120. PMID: 37590407, PMCID: PMC10450444, DOI: 10.1073/pnas.2309516120.
- Munc13 structural transitions and oligomers that may choreograph successive stages in vesicle priming for neurotransmitter releaseGrushin K, Kalyana Sundaram RV, Sindelar CV, Rothman JE. Munc13 structural transitions and oligomers that may choreograph successive stages in vesicle priming for neurotransmitter release. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2121259119. PMID: 35135883, PMCID: PMC8851502, DOI: 10.1073/pnas.2121259119.
- In Vitro Configuration of Munc13-1 Bridging of Phospholipid Bilayers at Resting ConditionsGrushin K, Sundaram R, Gibson K, Krishnakumar S, Sindelar C, Rothman J. In Vitro Configuration of Munc13-1 Bridging of Phospholipid Bilayers at Resting Conditions. Biophysical Journal 2020, 118: 400a. DOI: 10.1016/j.bpj.2019.11.2272.
- Structural Insight into the Interaction of Synaptotagmin-1 and Snare Complex on Lipid Bilayer by Cryo-Electron MicroscopyGrushin K, Wang J, Coleman J, Rothman J, Sindelar C, Krishnakumar S. Structural Insight into the Interaction of Synaptotagmin-1 and Snare Complex on Lipid Bilayer by Cryo-Electron Microscopy. Biophysical Journal 2018, 114: 282a. DOI: 10.1016/j.bpj.2017.11.1622.
- Reversible stacking of lipid nanodiscs for structural studies of clotting factorsGrushin K, White M, Stoilova-McPhie S. Reversible stacking of lipid nanodiscs for structural studies of clotting factors. Nanotechnology Reviews 2017, 6: 139-148. DOI: 10.1515/ntrev-2016-0073.
- Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5)Georgieva E, Borbat P, Grushin K, Stoilova-McPhie S, Kulkarni N, Liang Z, Freed J. Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5). Frontiers In Physiology 2016, 7: 317. PMID: 27524969, PMCID: PMC4965473, DOI: 10.3389/fphys.2016.00317.
- EPR and Electron Microscopy Study of the Influenza a M2 Transmembrane Domain Assembly and Drug ResponseGeorgieva E, Borbat P, Grushin K, Stoilova-McPhie S, Kulkarni N, Liang Z, Freed J. EPR and Electron Microscopy Study of the Influenza a M2 Transmembrane Domain Assembly and Drug Response. Biophysical Journal 2016, 110: 445a-446a. DOI: 10.1016/j.bpj.2015.11.2397.
- Factor VIII organisation on nanodiscs with different lipid compositionGrushin K, Miller J, Dalm D, Stoilova-McPhie S. Factor VIII organisation on nanodiscs with different lipid composition. Thrombosis And Haemostasis 2015, 113: 741-749. PMID: 25589466, DOI: 10.1160/th14-09-0725.
- Dimeric Organization of Blood Coagulation Factor VIII bound to Lipid NanotubesDalm D, Galaz-Montoya J, Miller J, Grushin K, Villalobos A, Koyfman A, Schmid M, Stoilova-McPhie S. Dimeric Organization of Blood Coagulation Factor VIII bound to Lipid Nanotubes. Scientific Reports 2015, 5: 11212. PMID: 26082135, PMCID: PMC4469981, DOI: 10.1038/srep11212.
- PS-GC Nanodiscs Assembly for Structural Studies of Coagulation Proteins and Their ComplexesGrushin K, Stoilova-McPhie S. PS-GC Nanodiscs Assembly for Structural Studies of Coagulation Proteins and Their Complexes. Biophysical Journal 2015, 108: 175a. DOI: 10.1016/j.bpj.2014.11.966.
- Membrane-Induced Dimerization of Coagulation Factor VIIIDalm D, Grushin K, Miller J, Pettitt M, Stoilova-McPhie S. Membrane-Induced Dimerization of Coagulation Factor VIII. Biophysical Journal 2015, 108: 39a. DOI: 10.1016/j.bpj.2014.11.243.
- Lipid nanotechnologies for structural studies of membrane‐associated proteinsStoilova‐McPhie S, Grushin K, Dalm D, Miller J. Lipid nanotechnologies for structural studies of membrane‐associated proteins. Proteins Structure Function And Bioinformatics 2014, 82: 2902-2909. PMID: 24957666, PMCID: PMC5292012, DOI: 10.1002/prot.24631.
- Helical organization of blood coagulation factor VIII on lipid nanotubes.Miller J, Dalm D, Koyfman A, Grushin K, Stoilova-McPhie S. Helical organization of blood coagulation factor VIII on lipid nanotubes. Journal Of Visualized Experiments 2014 PMID: 24961276, PMCID: PMC4126079, DOI: 10.3791/51254.
- Helical Organization of Blood Coagulation Factor VIII on Lipid NanotubesMiller J, Dalm D, Koyfman A, Grushin K, Stoilova-McPhie S. Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes. Journal Of Visualized Experiments 2014 DOI: 10.3791/51254-v.
- Lack of recombinant factor VIII B‐domain induces phospholipid vesicle aggregation: implications for the immunogenicity of factor VIIIGrushin K, Miller J, Dalm D, Parker E, Healey J, Lollar P, Stoilova-McPhie S. Lack of recombinant factor VIII B‐domain induces phospholipid vesicle aggregation: implications for the immunogenicity of factor VIII. Haemophilia 2014, 20: 723-731. PMID: 24750465, PMCID: PMC4149818, DOI: 10.1111/hae.12421.
- Structures of Blood Coagulation Factor VIII in Solution and Membrane-BoundKoyfman A, Miller J, Dalm D, Grushin K, Stoilova-McPhie S. Structures of Blood Coagulation Factor VIII in Solution and Membrane-Bound. Biophysical Journal 2014, 106: 635a. DOI: 10.1016/j.bpj.2013.11.3510.
- Resolving the Structural Basis of Factor VIII ActivationDalm D, Grushin K, Koyfman A, Miller J, Stoilova-McPhie S. Resolving the Structural Basis of Factor VIII Activation. Biophysical Journal 2014, 106: 599a. DOI: 10.1016/j.bpj.2013.11.3319.
- Helical Organization of Coagulation Factor VIII on Lipid NanotubesStoilova-McPhie S, Miller J, Dalm D, Grushin K. Helical Organization of Coagulation Factor VIII on Lipid Nanotubes. Biophysical Journal 2014, 106: 599a. DOI: 10.1016/j.bpj.2013.11.3315.
- Circadian phase‐dependent effect of nitric oxide on L‐type voltage‐gated calcium channels in avian cone photoreceptorsKo M, Shi L, Huang C, Grushin K, Park S, Ko G. Circadian phase‐dependent effect of nitric oxide on L‐type voltage‐gated calcium channels in avian cone photoreceptors. Journal Of Neurochemistry 2013, 127: 314-328. PMID: 23895452, PMCID: PMC4112736, DOI: 10.1111/jnc.12384.
- Structure of Membrane-Bound Porcine Factor VIIIDalm D, Miller J, Grushin K, Stoilova-McPhie S. Structure of Membrane-Bound Porcine Factor VIII. Biophysical Journal 2013, 104: 350a. DOI: 10.1016/j.bpj.2012.11.1943.
- Factor VIII Membrane-Bound OrganizationLeitch M, Miller J, Grushin K, Stoilova-McPhie S. Factor VIII Membrane-Bound Organization. Biophysical Journal 2012, 102: 393a. DOI: 10.1016/j.bpj.2011.11.2148.
- Membrane Bound Organization of Blood Coagulation Factor VIII FormsMiller J, Leitch M, Grushin K, Stoilova-McPhie S. Membrane Bound Organization of Blood Coagulation Factor VIII Forms. Biophysical Journal 2012, 102: 250a. DOI: 10.1016/j.bpj.2011.11.1377.
- “Arginine paradox” in cardiomyocytes of Sprague Dawley and spontaneously hypertensive rats: α2-adrenoreceptor-mediated regulation of L-type Ca2+ currents by L-arginineNenov M, Berezhnov A, Fedotova E, Grushin K, Pimenov O, Murashev A, Zinchenko V, Kokoz Y. “Arginine paradox” in cardiomyocytes of Sprague Dawley and spontaneously hypertensive rats: α2-adrenoreceptor-mediated regulation of L-type Ca2+ currents by L-arginine. Biochemistry (Moscow), Supplement Series A: Membrane And Cell Biology 2010, 4: 374-382. DOI: 10.1134/s1990747810040070.
- CIRCADIAN PROFILES IN THE EMBRYONIC CHICK HEART: L-TYPE VOLTAGE-GATED CALCIUM CHANNELS AND SIGNALING PATHWAYSKo M, Shi L, Grushin K, Nigussie F, Ko G. CIRCADIAN PROFILES IN THE EMBRYONIC CHICK HEART: L-TYPE VOLTAGE-GATED CALCIUM CHANNELS AND SIGNALING PATHWAYS. Chronobiology International 2010, 27: 1673-1696. PMID: 20969517, PMCID: PMC3155203, DOI: 10.3109/07420528.2010.514631.
- L-arginine Decreases L-type Ca2+ Current Through Receptor Activation Of NO-cGMP Cascade. Enigma Of “Arginine Paradox”Nenov M, Grushin K, Pimenov O, Dynnik V, Kokoz Y. L-arginine Decreases L-type Ca2+ Current Through Receptor Activation Of NO-cGMP Cascade. Enigma Of “Arginine Paradox”. Biophysical Journal 2009, 96: 172a-173a. DOI: 10.1016/j.bpj.2008.12.800.
- Role of the NO-cGMP cascade in regulation of L-type Ca2+ currents in isolated cardiomyocytesGrushin K, Nenov M, Dynnik V, Semushina S, Pakhomova I, Murashev A, Kokoz Y. Role of the NO-cGMP cascade in regulation of L-type Ca2+ currents in isolated cardiomyocytes. Biochemistry (Moscow), Supplement Series A: Membrane And Cell Biology 2008, 2: 243. DOI: 10.1134/s1990747808030082.
- Control of the L-type Ca2+ current by the NO-cGMP cascade in isolated cardiomyocytes of normotensive and spontaneously hypertensive ratsKokoz Y, Grushin K, Nenov M, Dynnik V, Semushina S, Pakhomova I, Murashev A. Control of the L-type Ca2+ current by the NO-cGMP cascade in isolated cardiomyocytes of normotensive and spontaneously hypertensive rats. Doklady Biochemistry And Biophysics 2007, 415: 170-173. PMID: 17933327, DOI: 10.1134/s1607672907040023.
- Stabilizing Role of Arginine and NO in the Regulation of Voltage-Sensitive L-type Ca2+ Current in CardiocytesDynnik V, Grushin K, Korystova A, Nenov M, Murashov A, Kokoz Y. Stabilizing Role of Arginine and NO in the Regulation of Voltage-Sensitive L-type Ca2+ Current in Cardiocytes. Doklady Biochemistry And Biophysics 2005, 404: 353-356. PMID: 16392755, DOI: 10.1007/s10628-005-0112-9.