W
Weihua Xue
Researcher at University of Nebraska Medical Center
Publications - 5
Citations - 251
Weihua Xue is an academic researcher from University of Nebraska Medical Center. The author has contributed to research in topics: Binding site & Serine hydrolase. The author has an hindex of 4, co-authored 5 publications receiving 230 citations.
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Journal ArticleDOI
Pseudo-esterase activity of human albumin: Slow turnover on tyrosine 411 and stable acetylation of 82 residues including 59 lysines
Oksana Lockridge,Weihua Xue,Andrea Gaydess,Hasmik Grigoryan,Shi Jian Ding,Lawrence M. Schopfer,Steven H. Hinrichs,Patrick Masson +7 more
TL;DR: The pseudo-esterase activity of albumin is the result of irreversible acetylation of 82 residues and is notThe result of turnover.
Journal ArticleDOI
Five tyrosines and two serines in human albumin are labeled by the organophosphorus agent FP-biotin.
Shi Jian Ding,John Carr,James Carlson,Larry Tong,Weihua Xue,Yifeng Li,Lawrence M. Schopfer,Bin Li,Florian Nachon,Oluwatoyin A. Asojo,Charles M. Thompson,Steven H. Hinrichs,Patrick Masson,Oksana Lockridge +13 more
TL;DR: The hypothesis that other residues in albumin could be modified by organophosphorus agents (OP) is investigated to help develop specific antibodies to detect OP exposure and to engineer albumin for use as an OP scavenger.
Journal ArticleDOI
Mass spectral characterization of organophosphate-labeled lysine in peptides.
TL;DR: Manual inspection of tandem mass spectrometry data led to the realization that lysines also make a covalent bond with OPs, suggesting that OP binding to lysine is a general phenomenon.
Journal ArticleDOI
Covalent binding of the organophosphorus agent FP-biotin to tyrosine in eight proteins that have no active site serine
Hasmik Grigoryan,Bin Li,Erica K. Anderson,Weihua Xue,Florian Nachon,Oksana Lockridge,Lawrence M. Schopfer +6 more
TL;DR: It is concluded that organophosphorus-reactive proteins include not only enzymes in the serine hydrolase family, but also proteins that have no active site serine, suggesting new directions to search for mechanisms of long-term effects of OP exposure.
Book ChapterDOI
Transglutaminase-mediated remodeling of the human erythrocyte membrane skeleton: relevance for erythrocyte diseases with shortened cell lifespan.
Laszlo Lorand,S. N. Prasanna Murthy,Anwar A. Khan,Weihua Xue,Oksana Lockridge,Athar H. Chishti +5 more
TL;DR: The human red blood cell transglutaminase (hRBC TG2) was the first in this family of enzymes for which an important role in cell–matrix interaction was found by demonstrating that the protein—when released from cells—could form an extremely tight complex with human fibronectin (FN).