Mitochondrial HSP60 (P1 protein) and a HSP70-like protein (mortalin) are major targets for modification during S-(1,1,2,2-tetrafluoroethyl)-L-cysteine-induced nephrotoxicity.-Reference-Cited by-同舟云学术

Mitochondrial HSP60 (P1 protein) and a HSP70-like protein (mortalin) are major targets for modification during S-(1,1,2,2-tetrafluoroethyl)-L-cysteine-induced nephrotoxicity.

Published:1993-11 Issue:31 Volume:268 Page:23157-23161
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bruschi S.A.,West K.A.,Crabb J.W.,Gupta R.S.,Stevens J.L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference40 articles.

1. Toxicity of the cysteine-S-conjugates and mercapturic acids of four structurally related difluoroethylenes in isolated proximal tubular cells from rat kidney

2. Detection of cysteine conjugate metabolite adduct formation with specific mitochondrial proteins using antibodies raised against halothane metabolite adducts.

3. Immunochemical detection of covalently modified kidney proteins in S-(1,1,2,2,-tetrafluoroethyl)-L-cysteine-treated rats

4. In vivo detection and characterization of protein adducts resulting from bioactivation of haloethene cysteine S-conjugates by fluorine-19 NMR: chlorotrifluoroethene and tetrafluoroethene

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