J
Jiansen Jiang
Researcher at National Institutes of Health
Publications - 44
Citations - 2192
Jiansen Jiang is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Chemistry & Biology. The author has an hindex of 21, co-authored 38 publications receiving 1664 citations. Previous affiliations of Jiansen Jiang include California NanoSystems Institute & Tsinghua University.
Papers
More filters
Journal ArticleDOI
Atomic structure of anthrax protective antigen pore elucidates toxin translocation
TL;DR: The structure of the protective antigen pore structure is determined by cryo-electron microscopy with direct electron counting and reveals the long-sought-after catalytic Φ-clamp and the membrane-spanning translocation channel, and supports the Brownian ratchet model for protein translocation.
Journal ArticleDOI
Structure of the full-length TRPV2 channel by cryo-EM
Kevin W. Huynh,Matthew R. Cohen,Jiansen Jiang,Amrita Samanta,David T. Lodowski,Z. Hong Zhou,Vera Y. Moiseenkova-Bell +6 more
TL;DR: The structure of full-length TRPV2 is determined at ∼5 Å resolution by cryo-electron microscopy and contains two constrictions, one each in the pore-forming upper and lower gates, which are proposed to contribute to diversity ofTRPV channels.
Journal ArticleDOI
Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly
Andrew P. AhYoung,Jiansen Jiang,Jiang Zhang,Xuan Khoi Dang,Joseph A. Loo,Z. Hong Zhou,Pascal F. Egea +6 more
TL;DR: The reconstitution and characterization of subcomplexes formed by the cytoplasm-exposed synaptotagmin-like mitochondrial lipid-binding protein (SMP) domains present in three of the five ERMES subunits are reported, suggesting a structure-based mechanism for the facilitated transport of phospholipids between organelles.
Journal ArticleDOI
Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
TL;DR: A mechanism for DegP to activate both functions via formation of large cage-like 12- and 24-mers after binding to substrate proteins is reported, which eliminates the inhibitory effects of the PDZ2 domain.
Journal ArticleDOI
Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.
Jiansen Jiang,Jiansen Jiang,Henry Chan,Darian D. Cash,Edward J. Miracco,Rachel R. Ogorzalek Loo,Heather Upton,Duilio Cascio,Duilio Cascio,Reid O’Brien Johnson,Kathleen Collins,Joseph A. Loo,Joseph A. Loo,Z. Hong Zhou,Z. Hong Zhou,Juli Feigon,Juli Feigon,Juli Feigon +17 more
TL;DR: Cryo–electron microscopy and x-ray crystallography is used to determine the structure of the Tetrahymena telomerase complex, a ribonucleoprotein complex that extends the telomere DNA at the 3′ ends of linear chromosomes, thereby counteracting the loss of DNA from replication and nucleolytic processing.