Sabrina S. Vollers

发表

De novo protein design enables the precise induction of RSV-neutralizing antibodies

Luciano A. Abriata, John T. Bates, Bruno E. Correia, 2020, Science.

Elucidation of Primary Structure Elements Controlling Early Amyloid β-Protein Oligomerization*

G. Bitan, D. Teplow, Sabrina S. Vollers, 2003, Journal of Biological Chemistry.

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.

M. Kirkitadze, G. Bitan, D. Teplow, 2002 .

distinct pathways Amyloid beta -protein (Abeta ) assembly: Abeta 40 and Abeta 42 oligomerize through

M. Kirkitadze, G. Bitan, D. Teplow, 2007 .

Identification and Analysis of the Domain Required for Trans-Acceleration Kinetics in the Human Glucose Transporter GLUT1: A Dissertation

Sabrina S Vollers, Sabrina S. Vollers, 2013 .

Sequence Determinants of GLUT1-mediated Accelerated-exchange Transport

Sabrina S Vollers, A. Carruthers, Sabrina S. Vollers, 2012, The Journal of Biological Chemistry.

Class II major histocompatibility complex tetramer staining: progress, problems, and prospects

L. Stern, Sabrina S Vollers, Sabrina S. Vollers, 2008, Immunology.

Minimal conformational plasticity enables TCR cross-reactivity to different MHC class II heterodimers

A. Sewell, P. Rizkallah, D. Cole, 2012, Scientific Reports.

A computationally designed chimeric antigen receptor provides a small-molecule safety switch for T-cell therapy

G. Coukos, B. Oh, P. Gainza, 2020, Nature Biotechnology.

Rosetta FunFolDes – A general framework for the computational design of functional proteins

Sarah Wehrle, Jaume Bonet, Thomas Krey, 2018, bioRxiv.

A computationally designed chimeric antigen receptor provides a small-molecule safety switch for T-cell therapy

G. Coukos, B. Oh, P. Gainza, 2020, Nature Biotechnology.

Amino Acid Position-specific Contributions to Amyloid β-Protein Oligomerization*

G. Bitan, D. Teplow, S. Maji, 2009, The Journal of Biological Chemistry.

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

M. Kirkitadze, G. Bitan, D. Teplow, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Amyloid b-protein (Ab) assembly: Ab40 and Ab42 oligomerize through distinct pathways

M. Kirkitadze, G. Bitan, D. Teplow, 2003 .

A molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization.

J. Straub, G. Bitan, D. Teplow, 2003, Journal of the American Chemical Society.

Amino Acid Position-specific Contributions to Amyloid

G. Bitan, D. Teplow, S. Maji, 2009 .

Determination of Peptide oligomerization state using rapid photochemical crosslinking.

G. Bitan, D. Teplow, Sabrina S. Vollers, 2005, Methods in molecular biology.

Amyloid (cid:1) -protein (A (cid:1) ) assembly: A (cid:1) 40 and A (cid:1) 42 oligomerize through distinct pathways

M. Kirkitadze, G. Bitan, D. Teplow, 2002 .

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.

M. Kirkitadze, G. Bitan, D. Teplow, 2003, Proceedings of the National Academy of Sciences of the United States of America.

De novo protein design enables precise induction of functional antibodies in vivo

B. Correia, P. Corthésy, J. Bates, 2020 .

Class II major histocompatibility complex tetramer staining: progress, problems, and prospects

L. Stern, Sabrina S. Vollers, 2008, Immunology.

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

M. Kirkitadze, G. Bitan, D. Teplow, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.

M. Kirkitadze, G. Bitan, D. Teplow, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Corrigendum

Sabrina S. Vollers, 2008 .