Chenxiang Lin, PhD
Professor of Cell Biology and of Biomedical EngineeringDownloadHi-Res Photo
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Cell Biology
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Additional Titles
Associate Director, Nanobiology Institute
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Appointments
Cell Biology
Primary
Additional Titles
Associate Director, Nanobiology Institute
Contact Info
Appointments
Cell Biology
Primary
Additional Titles
Associate Director, Nanobiology Institute
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About
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Titles
Professor of Cell Biology and of Biomedical Engineering
Associate Director, Nanobiology Institute
Appointments
Cell Biology
ProfessorPrimary
Other Departments & Organizations
Education & Training
- Research Fellow
- Harvard Medical School (2012)
- PhD
- Arizona State University (2009)
- BS
- Peking University (2004)
Research
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Overview
Medical Research Interests
Biophysics; Biosensing Techniques; Cell Biology; Cell Membrane; DNA; Lipid Bilayers; Membrane Fusion; Membranes, Artificial; Nanostructures; Nanotechnology; Nuclear Pore; Nucleic Acid Probes; Reference Standards
ORCID
0000-0001-7041-1946- View Lab Website
Chenxiang Lin Lab
Research at a Glance
Yale Co-Authors
Frequent collaborators of Chenxiang Lin's published research.
Publications Timeline
A big-picture view of Chenxiang Lin's research output by year.
Research Interests
Research topics Chenxiang Lin is interested in exploring.
Longfei Liu
Chunxiang Wu
C. Patrick Lusk, PhD
Erdem Karatekin, PhD
Yong Xiong, PhD
Ane Landajuela Larma
60Publications
5,427Citations
DNA
Nanostructures
Nanotechnology
Lipid Bilayers
Cell Membrane
Nuclear Pore
Publications
2025
DNA nanodevice for analysis of force-activated protein extension and interactions.
Zhou K, Chung M, Pandey S, Cheng J, Powell JT, Yan Q, Liu J, Xiong Y, Schwartz MA, Lin C. DNA nanodevice for analysis of force-activated protein extension and interactions. Nat Nanotechnol 2025 PMID: 41398070, DOI: 10.1038/s41565-025-02086-w.Peer-Reviewed Original ResearchKaryopherins remodel the dynamic organization of the nuclear pore complex transport barrier.
Kozai T, Fernandez-Martinez J, Kapinos LE, Gallardo P, van Eeuwen T, Saladin M, Eliasian R, Mazur A, Zhang W, Tempkin J, Panatala R, Delgado-Izquierdo M, Escribano-Marin R, Feng Q, Lin C, Sali A, Chait BT, Raveh B, Veenhoff LM, Rout MP, Lim RYH. Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier. Nat Cell Biol 2025 PMID: 41331088, DOI: 10.1038/s41556-025-01812-9.Peer-Reviewed Original Research
2024
Channel width modulates the permeability of DNA origami–based nuclear pore mimics
Feng Q, Saladin M, Wu C, Cao E, Zheng W, Zhang A, Bhardwaj P, Li X, Shen Q, Kapinos L, Kozai T, Mariappan M, Lusk C, Xiong Y, Lim R, Lin C. Channel width modulates the permeability of DNA origami–based nuclear pore mimics. Science Advances 2024, 10: eadq8773. PMID: 39536094, PMCID: PMC11559598, DOI: 10.1126/sciadv.adq8773.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsDNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force
Chung M, Zhou K, Powell J, Lin C, Schwartz M. DNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force. ACS Nano 2024, 18: 27590-27596. PMID: 39344156, PMCID: PMC11518680, DOI: 10.1021/acsnano.4c08663.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsTalin rod domainNegative-stain electron microscopyDouble-stranded DNADNA clampProtein functionRod domainCryptic sitesProtein interactionsMolecular clampCellular mechanotransductionStudy proteinsBiochemical studiesCell biologyAdult physiologyProtein conformationTalinProteinBiochemical scaleMultiple diseasesDNAARPC5LVinculinStructural analysisEmbryogenesisDNA-based devicesDNA nanoswitches pack an anti-cancer punch
Zhou K, Lin C. DNA nanoswitches pack an anti-cancer punch. Nature Nanotechnology 2024, 19: 1765-1766. PMID: 39209995, DOI: 10.1038/s41565-024-01749-4.Commentaries, Editorials and LettersCitationsLipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow
Zhang Y, Lin C. Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow. Current Opinion In Cell Biology 2024, 88: 102377. PMID: 38823338, PMCID: PMC11193448, DOI: 10.1016/j.ceb.2024.102377.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsCitationsAltmetricConceptsMembrane tensionLipid transportNonvesicular lipid transportLipid transfer proteinsOrganelle biogenesisLipid transferMembrane proteinsMembrane domainsLipid homeostasisBiological functionsLipid flowMembrane protein densityTransfer proteinMembrane regionsProtein densityProteinMembraneLipidBiogenesisOrganelles
2023
Recent Advances in DNA Origami-Engineered Nanomaterials and Applications
Zhan P, Peil A, Jiang Q, Wang D, Mousavi S, Xiong Q, Shen Q, Shang Y, Ding B, Lin C, Ke Y, Liu N. Recent Advances in DNA Origami-Engineered Nanomaterials and Applications. Chemical Reviews 2023, 123: 3976-4050. PMID: 36990451, PMCID: PMC10103138, DOI: 10.1021/acs.chemrev.3c00028.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsCitationsAltmetricMeSH Keywords and ConceptsConceptsDNA origami techniquePaul RothemundDNA nanotechnologyOrigami techniqueExciting achievementsNanomaterialsMaterials scienceRecent progressRecent advancesNanotechnologyUseful applicationsApplicationsRothemundSignificant advancesUnexplored research avenuesOriginal proposalFieldPhysicsMathematicsEngineeringAdvancesUnique fieldThe capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Shen Q, Kumari S, Xu C, Jang S, Shi J, Burdick R, Levintov L, Xiong Q, Wu C, Devarkar S, Tian T, Tripler T, Hu Y, Yuan S, Temple J, Feng Q, Lusk C, Aiken C, Engelman A, Perilla J, Pathak V, Lin C, Xiong Y. The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2202815120. PMID: 36943880, PMCID: PMC10068764, DOI: 10.1073/pnas.2202815120.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsHIV-1 capsidC-terminal tail regionTriple arginine motifNuclear pore complexPhenylalanine-glycine motifsBipartite motifNuclear importPore complexNuclear poresNuclear entryNup153Capsid latticeInteraction moduleProtein latticeCA assemblyCA hexamersIntact capsidsNucleoporinsHIV-1 coreMotifCapsidTail regionIntact formInfection studiesMechanistic evidenceModeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexesCLASP2 recognizes tubulins exposed at the microtubule plus-end in a nucleotide state–sensitive manner
Luo W, Demidov V, Shen Q, Girão H, Chakraborty M, Maiorov A, Ataullakhanov F, Lin C, Maiato H, Grishchuk E. CLASP2 recognizes tubulins exposed at the microtubule plus-end in a nucleotide state–sensitive manner. Science Advances 2023, 9: eabq5404. PMID: 36598991, PMCID: PMC9812398, DOI: 10.1126/sciadv.abq5404.Peer-Reviewed Original ResearchCitationsAltmetric
Academic Achievements & Community Involvement
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Honors
honor Odyssey Award
09/01/2020Regional AwardRichard and Susan Smith Family FoundationDetailsUnited Stateshonor Director's New Innovator Award
09/30/2014National AwardNational Institutes of HealthDetailsUnited States
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Chenxiang Lin Lab
Lab
West Campus Integrative Science & Technology Center
850 West Campus Drive, Rm 213
West Haven, CT 06516