Zobrazeno 1 - 10
of 185
pro vyhledávání: '"G. Kornhaber"'
The nature of flexibility in the helix-turn-helix region of E. coli trp aporepressor has been unexplained for many years. The original ensemble of nuclear magnetic resonance (NMR structures showed apparent disorder, but chemical shift and relaxation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca51d8ecd61df5d908416f83ff1e61d5
https://europepmc.org/articles/PMC5757375/
https://europepmc.org/articles/PMC5757375/
Autor:
Yong Xiang, Zhongwei Gao, Farhad Forouhar, Min Su, Lu Meng, Lance Wells, G. Kornhaber, Sahand Milaninia, Jayaraman Seetharaman, Kelley W. Moremen, Robert Bridger, David F. Thieker, Gaetano T. Montelione, Liang Tong, Annapoorani Ramiah, Parastoo Azadi, Lucas Veillon, Robert J. Woods, Heather A. Moniz
Publikováno v:
Journal of Biological Chemistry. 288:34680-34698
Background: Specificity and enzymology of glycan sialylation is poorly understood, despite its importance in biological recognition. Results: ST6GAL1 structure was determined, and substrate binding was modeled to probe active site specificity. Conclu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6635b45ef2cbe918967ffe99324bc3ee
https://doi.org/10.1074/jbc.m113.519041
https://doi.org/10.1074/jbc.m113.519041
Autor:
Keith Hamilton, Gaetano T. Montelione, Erik Procko, Min Su, James M. Aramini, David Baker, Liang Tong, Rickard Hedman, Jayaraman Seetharaman, John F. Hunt, G. Kornhaber, Sarel J. Fleishman
Publikováno v:
Journal of Molecular Biology. 425:3563-3575
While there has been considerable progress in designing protein-protein interactions, the design of proteins that bind polar surfaces is an unmet challenge. We describe the computational design of a protein that binds the acidic active site of hen eg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cbad3b695ffa29371dd390d722577a3
https://doi.org/10.1016/j.jmb.2013.06.035
https://doi.org/10.1016/j.jmb.2013.06.035
Autor:
Alexander P. Kuzin, Devin J. Noblin, Thomas Acton, Craig M. Crews, Liang Tong, G. Kornhaber, Gaetano T. Montelione, Scott Lew, Jayaraman Seetharaman, Taavi K. Neklesa, Rong Xiao
Publikováno v:
ACS Chemical Biology. 8:2293-2300
Small molecule control of intracellular protein levels allows temporal and dose-dependent regulation of protein function. Recently, we developed a method to degrade proteins fused to a mutant dehalogenase (HaloTag2) using small molecule hydrophobic t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a0d0faaf690fbb988c268e92152d156
https://doi.org/10.1021/cb400569k
https://doi.org/10.1021/cb400569k
Autor:
Thomas Acton, Seema Sharma, Ken Conover, Stephen Anderson, D. Lee, Saichu N. Tong, Colleen Ciccosanti, Yuanpeng J. Huang, Jessica Y. Locke, G. V. T. Swapna, Dayaban Patel, Paolo Rossi, Mei Jiang, Huang Wang, Rong Xiao, John K. Everett, Ritu Shastry, Lei Mao, W.A. Buchwald, Dongyan Wang, Li Zhao, James M. Aramini, Keith Hamilton, Melissa Maglaqui, Gaetano T. Montelione, Saheli Mitra, Li Chung Ma, G. Kornhaber, Haleema Janjua, Seema Sahdev, R.L. Belote
Publikováno v:
Journal of Structural Biology. 172:21-33
We describe the core Protein Production Platform of the Northeast Structural Genomics Consortium (NESG) and outline the strategies used for producing high-quality protein samples. The platform is centered on the cloning, expression and purification o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cef8ef3e3228ecdd23c96054ab56830
https://doi.org/10.1016/j.jsb.2010.07.011
https://doi.org/10.1016/j.jsb.2010.07.011
Autor:
Michael R. Slater, Thomas Acton, Kate Q. Zhao, Gaetano T. Montelione, G. V. T. Swapna, Ritu Shastry, Robin Hurst, G. Kornhaber, Li Zhao
Publikováno v:
Journal of Structural and Functional Genomics
Wheat germ cell-free methods provide an important approach for the production of eukaryotic proteins. We have developed a protein expression vector for the TNT® SP6 High-Yield Wheat Germ Cell-Free (TNT WGCF) expression system (Promega) that is also
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daaddd2907e63529eea87c1b573baec6
https://doi.org/10.1007/s10969-010-9093-8
https://doi.org/10.1007/s10969-010-9093-8
Autor:
G. Kornhaber, Brigitte Rigat, Michael B. Tropak, Deepangi Pandit, Liangiie Tang, Gustavo Maegawa, Maria Fuller, Justin D. Buttner, Yoshitomo Hamuro, Joe T.R. Clarke, Don J. Mahuran
Publikováno v:
Journal of Biological Chemistry. 284:23502-23516
Gaucher disease (GD), the most prevalent lysosomal storage disease, is caused by a deficiency of glucocerebrosidase (GCase). The identification of small molecules acting as agents for enzyme enhancement therapy is an attractive approach for treating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88a279672d869266e51f6bd850551cb2
https://doi.org/10.1074/jbc.m109.012393
https://doi.org/10.1074/jbc.m109.012393
Autor:
Yoshitomo Hamuro, Brigitte Rigat, Stephen J. Coales, Michael B. Tropak, Eric D. Brown, Don J. Mahuran, Gustavo Maegawa, Justin D. Buttner, Cecilia Murphy, G. Kornhaber, Steven J. Tuske, Jan E. Blanchard
Publikováno v:
ChemBioChem. 9:2650-2662
Point mutations in beta-glucocerebrosidase (GCase) can result in a deficiency of both GCase activity and protein in lysosomes thereby causing Gaucher Disease (GD). Enzyme inhibitors such as isofagomine, acting as pharmacological chaperones (PCs), inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a927cd89c75478a8487aee1b78cb41a
https://doi.org/10.1002/cbic.200800304
https://doi.org/10.1002/cbic.200800304
Publikováno v:
Journal of Biomolecular NMR. 34:259-269
Although a significant number of proteins include bound metals as part of their structure, the identification of amino acid residues coordinated to non-paramagnetic metals by NMR remains a challenge. Metal ligands can stabilize the native structure a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8fbf8e0b7f9ee84ebbfc2f55d036024
https://doi.org/10.1007/s10858-006-0027-5
https://doi.org/10.1007/s10858-006-0027-5
Autor:
G. Kornhaber, Phil Carter, Lan Ning, Burkhard Rost, Thomas Acton, Jinfeng Liu, Zeba Wunderlich, Gaetano T. Montelione, John Everett, Mark Gerstein, Nathaniel Echols
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 56:181-187
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::464b17ddd85280b1613c8c9e8f497f72
https://doi.org/10.1002/prot.20091
https://doi.org/10.1002/prot.20091