Functional annotation of human parvovirus b19 proteome and Molecular docking of VP1 protein with Teniposide [PDF]
, 2010 Parvovirus B19 is a common source of infection with a seroprevalence of 60-70% in the adult population. Human parvovirus causes several distinct clinical syndromes such as erythema, polyarthritis resembling rheumatoid arthritis, vasculitis, hydrops ...
Amburu Praneetha +3 more
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Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps. [PDF]
PLoS ONE, 2016 Cyclophilins are ubiquitous cis-trans-prolyl isomerases (PPIases) found in all kingdoms of life. Here, we identify a novel family of cyclophilins, termed AquaCyps, which specifically occurs in marine Alphaproteobacteria, but not in related terrestric ...
Roman P Jakob +4 more
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Cyclophilins A, B, and C Role in Human T Lymphocytes Upon Inflammatory Conditions
Frontiers in Immunology, 2021 Cyclophilins (Cyps) are a group of peptidyl-prolyl cis/trans isomerases that play crucial roles in regulatory mechanisms of cellular physiology and pathology in several inflammatory conditions.
Sandra Gegunde +8 more
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The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer
Biomolecules, 2018 Peptidyl prolyl isomerases (PPIases) are broadly expressed enzymes that accelerate the cis-trans isomerization of proline peptide bonds. The most extensively studied PPIase family member is protein interacting with never in mitosis A1 (PIN1), which ...
Stefano Stifani
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Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor. [PDF]
, 2006 The nematode Caenorhabditis elegans represents an excellent model in which to examine nematode gene expression and function. A completed genome, straightforward transgenesis, available mutants and practical genome-wide RNAi approaches provide an ...
Andrew J. Birnie +42 more
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Peptidyl-prolyl isomerases : A full cast of critical actors in cardiovascular diseases [PDF]
, 2015 Peptidyl-prolyl cis-trans-isomerases are a highly conserved family of immunophilins. The three peptidyl-prolyl cis-trans-isomerase subfamilies are cyclophilins, FK-506-binding proteins, and parvulins. Peptidyl-prolyl cis-trans-isomerases are expressed in
A. Gowran +5 more
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Calcineurin inhibitors: status quo and perspectives
Biomolecular Concepts, 2011 Despite the fact that cyclosporin A (CsA) and tacrolimus (FK506) are very potent drugs in the treatment of serious autoimmune diseases and in the prevention of graft vs.
Erdmann Frank, Weiwad Matthias
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Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. [PDF]
PLoS Biology, 2010 Peptidyl-prolyl isomerases catalyze the conversion between cis and trans isomers of proline. The cyclophilin family of peptidyl-prolyl isomerases is well known for being the target of the immunosuppressive drug cyclosporin, used to combat organ ...
Tara L Davis +11 more
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Peptidyl-prolyl cis/trans isomerases in GtoPdb v.2023.1
IUPHAR/BPS Guide to Pharmacology CITE, 2023 Peptidyl-prolyl cis/trans isomerases (PPIases) are an enzyme family which catalyse the cis/trans isomerisation of proline peptide bonds to promote the folding and re-folding of peptides and proteins. Three subfamilies have been identified: cyclophilins, FK506-binding proteins and parvulins.
Tracy Robson, Stephanie Annett
openaire +1 more source
, 2007 The nematode cuticle is an extremely flexible and resilient exoskeleton that permits locomotion via attachment to muscle, confers environmental protection and allows growth by molting.
Johnstone, I. J., Page, A. P.
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