G
G. Kornhaber
Researcher at Rutgers University
Publications - 19
Citations - 1355
G. Kornhaber is an academic researcher from Rutgers University. The author has contributed to research in topics: Structural genomics & Protein structure. The author has an hindex of 13, co-authored 19 publications receiving 1223 citations. Previous affiliations of G. Kornhaber include Structural Genomics Consortium & Center for Advanced Biotechnology and Medicine.
Papers
More filters
Journal ArticleDOI
Identification and characterization of ambroxol as an enzyme enhancement agent for Gaucher disease.
Gustavo Maegawa,Michael B. Tropak,Justin D. Buttner,Brigitte Rigat,Maria Fuller,Deepangi Pandit,Liangiie Tang,G. Kornhaber,Yoshitomo Hamuro,Joe T.R. Clarke,Don J. Mahuran +10 more
TL;DR: Ambroxol (ABX), a drug used to treat airway mucus hypersecretion and hyaline membrane disease in newborns, was identified and found to be a pH-dependent, mixed-type inhibitor of GCase, and modeling studies indicated that ABX interacts with both active and non-active site residues.
Journal ArticleDOI
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
Theresa Ramelot,John R. Cort,John R. Cort,Sharon Goldsmith-Fischman,Sharon Goldsmith-Fischman,G. Kornhaber,G. Kornhaber,G. Kornhaber,Rong Xiao,Rong Xiao,Ritu Shastry,Ritu Shastry,Thomas Acton,Thomas Acton,Barry Honig,Barry Honig,Gaetano T. Montelione,Gaetano T. Montelione,Gaetano T. Montelione,Michael A. Kennedy,Michael A. Kennedy +20 more
TL;DR: Structural and functional similarities, genomic context in operons containing other homologous genes, and distributions of conserved surface residues support the hypothesis that IscU protein domains are homologueous with the SufE/YgdK family of [Fe-S] cluster assembly proteins.
Journal ArticleDOI
Computational design of catalytic dyads and oxyanion holes for ester hydrolysis.
Florian Richter,Rebecca Blomberg,Sagar D. Khare,Gert Kiss,Alexandre P. Kuzin,Adam J. T. Smith,Jasmine L. Gallaher,Zbigniew Pianowski,Roger C. Helgeson,Alexej Grjasnow,Rong Xiao,Jayaraman Seetharaman,Min Su,Sergey M. Vorobiev,Scott Lew,Farhad Forouhar,G. Kornhaber,John F. Hunt,Gaetano T. Montelione,Liang Tong,Kendall N. Houk,Donald Hilvert,David Baker +22 more
TL;DR: Kinetic experiments indicate that the active site cysteines are rapidly acylated as programmed by design, but the subsequent slow hydrolysis of the acyl-enzyme intermediate limits overall catalytic efficiency, which highlights the challenges that computational design must overcome to achieve high levels of activity.
Journal ArticleDOI
The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium
Rong Xiao,Stephen Anderson,James M. Aramini,R.L. Belote,W.A. Buchwald,Colleen Ciccosanti,Ken Conover,John K. Everett,Keith Hamilton,Yuanpeng J. Huang,Haleema Janjua,Mei Jiang,G. Kornhaber,D. Lee,Jessica Y. Locke,Li Chung Ma,Melissa Maglaqui,Lei Mao,Saheli Mitra,Dayaban Patel,Paolo Rossi,Seema Sahdev,Seema Sharma,Ritu Shastry,G. V. T. Swapna,Saichu N. Tong,Dongyan Wang,Huang Wang,Li Zhao,Gaetano T. Montelione,Thomas Acton +30 more
TL;DR: The core Protein Production Platform of the Northeast Structural Genomics Consortium (NESG) is described and the strategies used for producing high-quality protein samples are outlined, centered on the cloning, expression and purification of 6X-His-tagged proteins using T7-based Escherichia coli systems.
Journal ArticleDOI
Enzymatic Basis for N-Glycan Sialylation STRUCTURE OF RAT α2,6-SIALYLTRANSFERASE (ST6GAL1) REVEALS CONSERVED AND UNIQUE FEATURES FOR GLYCAN SIALYLATION
Lu Meng,Farhad Forouhar,David F. Thieker,Zhongwei Gao,Annapoorani Ramiah,Heather A. Moniz,Yong Xiang,Jayaraman Seetharaman,Sahand Milaninia,Min Su,Robert Bridger,Lucas Veillon,Parastoo Azadi,G. Kornhaber,G. Kornhaber,Lance Wells,Gaetano T. Montelione,Gaetano T. Montelione,Robert J. Woods,Robert J. Woods,Liang Tong,Kelley W. Moremen +21 more
TL;DR: The enzymatic basis for glycan sialylation in animal systems is examined by determining the crystal structures of rat ST6GAL1, an enzyme that creates terminal α2,6-sialic acid linkages on complex-type N-glycans at 2.4 Å resolution.