Results 31 to 40 of about 4,905 (211)
Mycobacterium tuberculosis Peptidyl-Prolyl Isomerases Also Exhibit Chaperone like Activity In-Vitro and In-Vivo. [PDF]
PLoS ONE, 2016 Peptidyl-prolyl cis-trans isomerases (Ppiases), also known as cyclophilins, are ubiquitously expressed enzymes that assist in protein folding by isomerization of peptide bonds preceding prolyl residues.
Saurabh Pandey +8 more
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Genome biology, 2005 Cyclophilins (Enzyme Commission (EC) number 5.1.2.8) belong to a group of proteins that have peptidyl-prolyl cis-trans isomerase activity; such proteins are collectively known as immunophilins and also include the FK-506-binding proteins and the parvulins. Cyclophilins are found in all cells of all organisms studied, in both prokaryotes and eukaryotes;
Wang, Ping, Heitman, Joseph
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Viruses, 2012 The advent of the replicon system together with advances in cell culture have contributed significantly to our understanding of the function of virally-encoded structural and nonstructural proteins in the replication cycle of the hepatitis C virus.
Philippe Gallay, Sam Hopkins
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Cyclophilin D links programmed cell death and organismal aging in Podospora anserina [PDF]
, 2018 This is the final version of the article. Available from Wiley via the DOI in this record.Cyclophilin D (CYPD) is a mitochondrial peptidyl prolyl-cis,trans-isomerase involved in opening of the mitochondrial permeability transition pore (mPTP).
Breunig, C +5 more
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Nature Communications, 2016 Cyclophilins play a key role in the life cycle of many viruses and represent important drug targets for broad-spectrum antiviral therapies. Here, the authors use fragment-based drug discovery to develop non-peptidic inhibitors of human cyclophilins with ...
Abdelhakim Ahmed-Belkacem +12 more
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Frontiers in Pharmacology, 2018 The Clostridium botulinum C2 toxin is an exotoxin causing severe enterotoxic symptoms. The C2 toxin consists of the binding/translocation component C2II, and the enzymatic active component C2I.
Katharina Ernst +3 more
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Scientific Reports, 2021 Peptidyl-prolyl cis–trans isomerases (PPIases) are the only class of enzymes capable of cis–trans isomerization of the prolyl peptide bond. The PPIases, comprising of different families viz., cyclophilins, FK506-binding proteins (FKBPs), parvulins and ...
Mangaljeet Singh +9 more
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Native State Proline Isomerization: An Intrinsic Molecular Switch [PDF]
, 2003 Exquisite control of biological function is achieved via tight regulation of the catalytic and binding activities of cellular proteins. The mechanistic details of protein regulation vary from targeted chemical modification of amino acid side chains (1 ...
Andreotti, Amy, Andreotti, Amy
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The Arabidopsis Cyclophilin Gene Family [PDF]
Plant Physiology, 2004 AbstractDatabase searching has allowed the identification of a number of previously unreported single and multidomain isoform members of the Arabidopsis cyclophilin gene family. In addition to the cyclophilin-like peptidyl-prolyl cis-trans isomerase domain, the latter contain a variety of other domains with characterized functions.
Patrick G N, Romano +2 more
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Structural and Functional Insights into Human Nuclear Cyclophilins
Biomolecules, 2018 The peptidyl prolyl isomerases (PPI) of the cyclophilin type are distributed throughout human cells, including eight found solely in the nucleus. Nuclear cyclophilins are involved in complexes that regulate chromatin modification, transcription, and pre ...
Caroline Rajiv, Tara L. Davis
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