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Cited by 386

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition

Open access
WOODFIELD, Kuei, RÜCK, Alexander, BRDICZKA, Dieter, HALESTRAP, Andrew P.·1998·Biochemical Journal

Abstract

A fusion protein between cyclophilin-D (CyP-D) and glutathione S-transferase (GST) was shown to bind to purified liver inner mitochondrial membranes (IMMs) in a cyclosporin A (CsA)-sensitive manner. Binding was enhanced by diamide treatment of the IMMs. Immobilized GST–CyP-D avidly bound a single 30 kDa protein present in Triton X-100-solubilized IMMs; immunoblotting showed this to be the adenine nucleotide translocase (ANT). Binding was prevented by pretreatment of the CyP-D with CsA, but not with cyclosporin H. Purified ANT also bound specifically to GST–CyP-D, but porin did not, even in the presence of ANT.

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Crossref · 10.1042/bj3360287

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Metadata

Authors
WOODFIELD, K., RÜCK, A., BRDICZKA, D., & HALESTRAP, A. P.
Venue
Biochemical Journal
Published
1998-12-01
Volume
336
Issue
2
Pages
287-290
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W1909302202
Cited by
386
References
1
FWCI
4.95
Type
journal article
Language
en
Open access
bronze

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WOODFIELD, K., RÜCK, A., BRDICZKA, D., & HALESTRAP, A. P. (1998). Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Biochemical Journal. https://doi.org/10.1042/bj3360287

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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