P41GM103403

NIH – National Institute of General Medical Sciences

An antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses

Liu, L., Iketani, S., Guo, Y., Reddem, E. R., Casner, R. G., Nair, M. S., Yu, J., Chan, J. F.-W., Wang, M., Cerutti, G., Li, Z., Morano, N. C., Castagna, C. D., Corredor, L., Chu, H., Yuan, S., Poon, V. K.-M., Chan, C. C.-S., Chen, Z., … Ho, D. D. (2022). An antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses. Science Translational Medicine, 14(646). https://doi.org/10.1126/scitranslmed.abn6859
Authors:
Lihong Liu
Sho Iketani
Yicheng Guo
Eswar R. Reddem
Ryan G. Casner
Manoj S. Nair
Jian Yu
Jasper F.-W. Chan
Maple Wang
Gabriele Cerutti
Zhiteng Li
Nicholas C. Morano
Candace D. Castagna
Laura Corredor
Hin Chu
Shuofeng Yuan
Vincent Kwok-Man Poon
Chris Chun-Sing Chan
Zhiwei Chen
Yang Luo
Marcus Cunningham
Alejandro Chavez
Michael T. Yin
David S. Perlin
Moriya Tsuji
Kwok-Yung Yuen
Peter D. Kwong
Zizhang Sheng
Yaoxing Huang
Lawrence Shapiro
David D. Ho
Affiliated Authors:
Lihong Liu
Sho Iketani
Yicheng Guo
Eswar R. Reddem
Ryan G. Casner
Manoj S. Nair
Jian Yu
Maple Wang
Gabriele Cerutti
Zhiteng Li
Nicholas C. Morano
Candace D. Castagna
Laura Corredor
Yang Luo
Alejandro Chavez
Michael T. Yin
Moriya Tsuji
Kwok-Yung Yuen
Peter D. Kwong
Zizhang Sheng
Yaoxing Huang
Lawrence Shapiro
David D. Ho
Grants:
ZIAAI005022 (NIH – National Institute of Allergy and Infectious Diseases)
ZIAAI005149 (NIH – National Institute of Allergy and Infectious Diseases)
P41GM103403 (NIH – National Institute of General Medical Sciences)
S10OD020056 (NIH – Office of the Director, National Institutes of Health)
Publication Type:
Article
Unique ID:
10.1126/scitranslmed.abn6859
PMID:
Publication Date:
Data Source:
Scopus

Record Created:

How clustered protocadherin binding specificity is tuned for neuronal self-/nonself-recognition

Goodman, K. M., Katsamba, P. S., Rubinstein, R., Ahlsén, G., Bahna, F., Mannepalli, S., Dan, H., Sampogna, R. V., Shapiro, L., & Honig, B. (2022). How clustered protocadherin binding specificity is tuned for neuronal self-/nonself-recognition. ELife, 11. CLOCKSS. https://doi.org/10.7554/elife.72416
Authors:
Kerry Marie Goodman
Phinikoula S Katsamba
Rotem Rubinstein
Göran Ahlsén
Fabiana Bahna
Seetha Mannepalli
Hanbin Dan
Rosemary V Sampogna
Lawrence Shapiro
Barry Honig
Affiliated Authors:
Kerry Marie Goodman
Phinikoula S Katsamba
Göran Ahlsén
Fabiana Bahna
Seetha Mannepalli
Hanbin Dan
Rosemary V Sampogna
Lawrence Shapiro
Barry Honig
Subjects:
Author Keywords:
protocadherins
self-recognition
neuronal self-avoidance
trans interactions
cis interactions
crystal structure
mouse
molecular biophysics
neuroscience
structural biology
Grants:
R01DK106548 (NIH – National Institute of Diabetes and Digestive and Kidney Diseases)
P41GM103403 (NIH – National Institute of General Medical Sciences)
R01MH114817 (NIH – National Institute of Mental Health)
Publication Type:
Article
Unique ID:
10.7554/elife.72416
PMID:
Journal:
Publication Date:
Data Source:
PubMed

Record Created:

Conformational equilibria in allosteric control of Hsp70 chaperones

Wang, W., Liu, Q., Liu, Q., & Hendrickson, W. A. (2021). Conformational equilibria in allosteric control of Hsp70 chaperones. Molecular Cell, 81(19), 3919-3933.e7. https://doi.org/10.1016/j.molcel.2021.07.039
Authors:
Wei Wang
Wayne A. Hendrickson
Qinglian Liu
Qun Liu
Affiliated Authors:
Wei Wang
Wayne A. Hendrickson
Author Keywords:
dnak
hsp70
allosteric regulation
crystal structure
molecular chaperone
protein folding
Grants:
R21AI140006 (NIH – National Institute of Allergy and Infectious Diseases)
R01GM107462 (NIH – National Institute of General Medical Sciences)
P41GM103403 (NIH – National Institute of General Medical Sciences)
P30GM124165 (NIH – National Institute of General Medical Sciences)
R01GM098592 (NIH – National Institute of General Medical Sciences)
Publication Type:
Article
Unique ID:
10.1016/j.molcel.2021.07.039
PMID:
Journal:
Publication Date:
Data Source:
Web of Science

Record Created:

Intermediates in allosteric equilibria of DnaK-ATP interactions with substrate peptiaes

Wang, W., & Hendrickson, W. A. (2021). Intermediates in allosteric equilibria of DnaK–ATP interactions with substrate peptides. Acta Crystallographica Section D Structural Biology, 77(5), 606–617. https://doi.org/10.1107/s2059798321002436
Authors:
Wei Wang
Wayne A. Hendrickson
Affiliated Authors:
Wei Wang
Wayne A. Hendrickson
Author Keywords:
allostery
atp hydrolysis
conformational transition
molecular chaperones
polypeptide clients
protein folding
Grants:
R01GM107462 (NIH – National Institute of General Medical Sciences)
P41GM103403 (NIH – National Institute of General Medical Sciences)
P30GM124165 (NIH – National Institute of General Medical Sciences)
Publication Type:
Article
Unique ID:
10.1107/S2059798321002436
PMID:
Publication Date:
Data Source:
Web of Science

Record Created: