Keyword search (4,163 papers available)

"Tao L" Authored Publications:

Title Authors PubMed ID
1 Protocol for a partially nested randomised controlled trial to evaluate the effectiveness of the scleroderma patient-centered intervention network COVID-19 home-isolation activities together (SPIN-CHAT) program to reduce anxiety among at-risk scleroderma patients. Thombs BD, Kwakkenbos L, Carrier ME, Bourgeault A, Tao L, Harb S, Gagarine M, Rice D, Bustamante L, Ellis K, Duchek D, Wu Y, Bhandari PM, Neupane D, Carboni-Jiménez A, Henry RS, Krishnan A, Sun Y, Levis B, He C, Turner KA, Benedetti A, Culos-Reed N, El-Baalbaki G, Hebblethwaite S, Bartlett SJ, Dyas L, Patten S, Varga J, Scleroderma Patient-centered Intervention Network (SPIN) COVID-19 Patient Advisory Team, SPIN Investigators 32521358
PSYCHOLOGY
2 S-nitrosation of Ca(2+)-loaded and Ca(2+)-free recombinant calbindin D(28K) from human brain. Tao L, Murphy ME, English AM 11994015
CHEMBIOCHEM
3 Mechanism of S-nitrosation of recombinant human brain calbindin D28K. Tao L, English AM 12641465
CHEMBIOCHEM
4 Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione. Tao L, English AM 15049710
CHEMBIOCHEM

 

Title:Mechanism of S-nitrosation of recombinant human brain calbindin D28K.
Authors:Tao L,  English AM
Link:https://www.ncbi.nlm.nih.gov/pubmed/12641465?dopt=Abstract
DOI:10.1021/bi0269963
Publication:Biochemistry
Keywords:
PMID:12641465 Category:Biochemistry Date Added:2019-06-20
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve Boulevard West, Montreal, Quebec, Canada H3G 1M8.

Description:

Mechanism of S-nitrosation of recombinant human brain calbindin D28K.

Biochemistry. 2003 Mar 25;42(11):3326-34

Authors: Tao L, English AM

Abstract

Mass spectrometry and UV-vis absorption results support a mechanism for NO donation by S-nitrosoglutathione (GSNO) to recombinant human brain calbindin D(28K) (rHCaBP) that requires the presence of trace copper, added as either Cu,Zn-superoxide dismutase (CuZnSOD) or CuSO(4). The extent of copper-catalyzed rHCaBP S-nitrosation depends on the ratio of protein to GSNO and on the reaction time, and NO-transfer is prevented when copper chelators are present. CuZnSOD is an efficient catalyst of rHCaBP S-nitrosation, and the mechanism of CuZnSOD-catalyzed S-nitrosation involves reduction of the active-site Cu(II) by a number of the five free thiols in rHCaBP, giving rise to thiyl radicals. The Cu(I)ZnSOD formed catalyzes the reductive cleavage of GSNO present in solution to give GSH and release NO. rHCaBP thiyl radicals react with NO to yield the S-nitrosoprotein. Cu(II)ZnSOD is also reduced by GSH in a concentration-dependent manner up to 5 mM but not at higher GSH concentrations. However, unlike the rHCaBP thiyl radicals, GS(*) radicals dimerize to GSSG faster than their reaction with NO. The data presented here provide a biologically relevant mechanism for protein S-nitrosation by small S-nitrosothiols. S-nitrosation is rapidly gaining recognition as a major form of protein posttranslational modification, and the efficient S-nitrosation of CaBP by CuZnSOD/GSNO is speculated to be of neurochemical importance given that CaBP and CuZnSOD are abundant in neurons.

PMID: 12641465 [PubMed - indexed for MEDLINE]




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