Results 11 to 20 of about 35,749 (233)

Non‐Immunosuppressive Cyclophilin Inhibitors [PDF]

open access: yesAngewandte Chemie International Edition, 2022
AbstractCyclophilins, enzymes with peptidyl‐prolyl cis/trans isomerase activity, are relevant to a large variety of biological processes. The most abundant member of this enzyme family, cyclophilin A, is the cellular receptor of the immunosuppressive drug cyclosporine A (CsA).
Cordelia Schiene‐Fischer   +2 more
openaire   +5 more sources

Cyclophilin‐B is an abundant protein whose conformation is similar to cyclophilin‐A [PDF]

open access: yesFEBS Letters, 1994
Cyclophilin‐B (bCyP‐20) was isolated in a relatively high quantity from calf brain and spleen tissues consecutively applying weak cation exchange, chromatofocusing and strong cation exchange chromatographies. Edman degradation yielded the N‐terminal sequence NH2‐DEKKKGPKVTVK‐VYFDLRIGDEDIGRVVIGLFGKTVPKTVDNFVAL.
Galat, Andrzej, Bouet, Françoise
openaire   +3 more sources

Cyclophilin D in mitochondrial pathophysiology

open access: yesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2010
Cyclophilins are a family of peptidyl-prolyl cis-trans isomerases whose enzymatic activity can be inhibited by cyclosporin A. Sixteen cyclophilins have been identified in humans, and cyclophilin D is a unique isoform that is imported into the mitochondrial matrix.
GIORGIO, VALENTINA   +6 more
openaire   +8 more sources

Cyclophilin B serum levels present variations across the menstrual cycle

open access: yesScientific Reports, 2023
Cyclophilins are a family of chaperones involved in inflammation and cell death. Cyclophilin B is released by inflammatory cells and acts through the receptor CD147, affecting matrix metalloproteases release, whilst cyclophilin D participates in hypoxia ...
Rebeca Alvariño   +7 more
doaj   +2 more sources

Stereo views of cocrystal structures of cyclophilins with cyclophilin inhibitors.pdf

open access: yes, 2016
Cocrystal structures (stereo views of sections of the electron density maps) of cyclophilin D complexed with different compounds from a new family of nonpeptidic, small-molecule cyclophilin ...
Jean-Michel Pawlotsky   +12 more
openaire   +2 more sources

Inhibitors of Cyclophilin A: Current and Anticipated Pharmaceutical Agents for Inflammatory Diseases and Cancers

open access: yesMolecules
Cyclophilin A, a widely prevalent cellular protein, exhibits peptidyl-prolyl cis-trans isomerase activity. This protein is predominantly located in the cytosol; additionally, it can be secreted by the cells in response to inflammatory stimuli ...
Xuemei Zhao   +3 more
doaj   +2 more sources

Thermo‐kinetic analysis space expansion for cyclophilin‐ligand interactions – identification of a new nonpeptide inhibitor using Biacore™ T200 [PDF]

open access: yesFEBS Open Bio, 2017
We have established a refined methodology for generating surface plasmon resonance sensor surfaces of recombinant his‐tagged human cyclophilin‐A. Our orientation‐specific stabilisation approach captures his‐tagged protein under ‘physiological conditions’
Martin A. Wear   +4 more
doaj   +2 more sources

Diagnostic Value of Cyclophilin A in Acute Ischemic Stroke [PDF]

open access: yesEurasian Journal of Emergency Medicine, 2017
Aim: The early diagnosis and treatment of patients presenting to the emergency department symptoms of stroke can significantly reduce mortality and morbidity rates associated with it.
Yunus Karaca   +9 more
doaj   +3 more sources

Cyclophilin A Isomerisation of Septin 2 Mediates Abscission during Cytokinesis

open access: yes, 2023
International audienceThe isomerase activity of Cyclophilin A is important for midbody abscission during cell division, however, to date, midbody substrates remain unknown.
Mc Gee, Margaret, M   +15 more
core   +2 more sources

s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin [PDF]

open access: yes, 1992
Cyclophilins (cyclosporin A-binding proteins) are conserved, ubiquitous, and abundant proteins that accelerate the isomerization of XaaPro peptide bonds and the refolding of proteins in vitro.
Arber, S.   +6 more
core   +1 more source

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