Calvin Yip
Calvin Yip
Associate Professor of Biochemistry and Molecular Biology, the University of British Columbia
Verified email at - Homepage
Cited by
Cited by
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
DJ Klionsky, AK Abdel-Aziz, S Abdelfatah, M Abdellatif, A Abdoli, S Abel, ...
autophagy 17 (1), 1-382, 2021
Accurate prediction of protein structures and interactions using a three-track neural network
M Baek, F DiMaio, I Anishchenko, J Dauparas, S Ovchinnikov, GR Lee, ...
Science 373 (6557), 871-876, 2021
Structure of the human mTOR complex I and its implications for rapamycin inhibition
CK Yip, K Murata, T Walz, DM Sabatini, SA Kang
Molecular cell 38 (5), 768-774, 2010
Structural characterization of the molecular platform for type III secretion system assembly
CK Yip, TG Kimbrough, HB Felise, M Vuckovic, NA Thomas, RA Pfuetzner, ...
Nature 435 (7042), 702-707, 2005
Salmonella effectors within a single pathogenicity island are differentially expressed and translocated by separate type III secretion systems
LA Knodler, J Celli, WD Hardt, BA Vallance, C Yip, BB Finlay
Molecular microbiology 43 (5), 1089-1103, 2002
A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system
T Spreter, CK Yip, S Sanowar, I André, TG Kimbrough, M Vuckovic, ...
Nature structural & molecular biology 16 (5), 468-476, 2009
A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1
Y Ren, CK Yip, A Tripathi, D Huie, PD Jeffrey, T Walz, FM Hughson
Cell 139 (6), 1119-1129, 2009
The monopolin complex crosslinks kinetochore components to regulate chromosome-microtubule attachments
KD Corbett, CK Yip, LS Ee, T Walz, A Amon, SC Harrison
Cell 142 (4), 556-567, 2010
Structural characterization of a type III secretion system filament protein in complex with its chaperone
CK Yip, BB Finlay, NCJ Strynadka
Nature structural & molecular biology 12 (1), 75-81, 2005
CesT is a multi‐effector chaperone and recruitment factor required for the efficient type III secretion of both LEE‐and non‐LEE‐encoded effectors of enteropathogenic …
NA Thomas, W Deng, JL Puente, EA Frey, CK Yip, NCJ Strynadka, ...
Molecular microbiology 57 (6), 1762-1779, 2005
Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation
K Mao, LH Chew, Y Inoue-Aono, H Cheong, U Nair, H Popelka, CK Yip, ...
Proceedings of the National Academy of Sciences 110 (31), E2875-E2884, 2013
Structure of EspB from the ESX-1 type VII secretion system and insights into its export mechanism
M Solomonson, D Setiaputra, KAT Makepeace, E Lameignere, ...
Structure 23 (3), 571-583, 2015
New structural insights into the bacterial type III secretion system
CK Yip, NCJ Strynadka
Trends in biochemical sciences 31 (4), 223-230, 2006
Molecular architecture of the TRAPPII complex and implications for vesicle tethering
CK Yip, J Berscheminski, T Walz
Nature structural & molecular biology 17 (11), 1298-1304, 2010
Molecular organization of the COG vesicle tethering complex
JA Lees, CK Yip, T Walz, FM Hughson
Nature structural & molecular biology 17 (11), 1292-1297, 2010
Beclin 1-Vps34 complex architecture: Understanding the nuts and bolts of therapeutic targets
DH Morris, CK Yip, Y Shi, BT Chait, QJ Wang
Frontiers in biology 10, 398-426, 2015
Properties of CD34+ CML stem/progenitor cells that correlate with different clinical responses to imatinib mesylate
X Jiang, D Forrest, F Nicolini, A Turhan, J Guilhot, C Yip, T Holyoake, ...
Blood, The Journal of the American Society of Hematology 116 (12), 2112-2121, 2010
Conformational flexibility and subunit arrangement of the modular yeast Spt-Ada-Gcn5 acetyltransferase complex
D Setiaputra, JD Ross, S Lu, DT Cheng, MQ Dong, CK Yip
Journal of Biological Chemistry 290 (16), 10057-10070, 2015
High intrinsic mechanical flexibility of mouse prion nanofibrils revealed by measurements of axial and radial Young’s moduli
G Lamour, CK Yip, H Li, J Gsponer
ACS nano 8 (4), 3851-3861, 2014
Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa
W Wu, D Sinha, S Shikov, CK Yip, T Walz, PC Billings, JD Lear, PN Walsh
Journal of biological chemistry 283 (27), 18655-18664, 2008
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