Includes bibliographical references (p. 65-101).
|Statement||Andrzej Galat, Sylvie Rivière.|
|LC Classifications||QP616.P46 G35 1998|
|The Physical Object|
|Pagination||117 p. :|
|Number of Pages||117|
|LC Control Number||98023127|
Among the foldases, peptidyl prolyl cis/trans isomerases (PPIases) catalyze the isomerization between the cis and trans forms of peptide bonds, Author: Weilin Lin, Malte Bonin, Annett Boden, Robert Wieduwild, Priyanka Murawala, Martin Wermke, Helena An. Peptidyl-prolyl cis/trans isomerases (PPIases) as a family of proteins are present in a range of species, display a multi-domain structure and, with an affinity for proline residues, are involved in This volume presents details of their structure and function. A short term for peptidyl prolyl cis/trans isomerization is prolyl isomerization. According to the recommendations of the Nomenclature Committee of the IU/BMB, enzymes catalyzing prolyl isomerization were named peptidyl prolyl cis/trans isomerases in The colloquial terms prolyl isomerase and proline isomerase are frequently in use. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB "Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes." Kontopidis G., .
Peptidyl-prolyl cis/trans isomerases (PPIases), a unique family of molecular chaperones, regulate protein folding at proline residues. These residues are abundant within intrinsically disordered proteins, like the microtubule-associated protein tau. Tau has been shown to become hyperphosphorylated and accumulate as one of the two main pathological hallmarks in Alzheimer's disease (AD), the Cited by: Karl-Josef Dietz, in International Review of Cytology, 9 Potential Role for Cyclophilins. Peptidyl-prolyl-cis⧸trans isomerases (PPIase) catalyze the isomerization of the peptide bond between a prolyl residue and the neighboring amino acid, which frequently is a bulky and lipophilic residue such as phenylalanine (Fischer et al., ).Without catalysis, the isomerization reaction occurs. Abstract. Peptidyl-prolyl cis-trans-isomerases are a highly conserved family of three peptidyl-prolyl cis-trans-isomerase subfamilies are cyclophilins, FKbinding proteins, and yl-prolyl cis-trans-isomerases are expressed in multiple human tissues and regulate different cellular functions, e.g. calcium handling, protein folding, and gene by: The target proteins for CsA and FK were found to be cyclophilins and FKbinding proteins, (FKBPs), respectively. They are unrelated in primary sequence, although both are peptidyl-prolyl cis-trans isomerases catalyzing the interconversion of Cited by:
Peptidyl-prolyl isomerases (PPIs) catalyse the cis-trans isomerisation of peptide bonds N-terminal to proline residues in polypeptide chains. They have roles in the folding of newly synthesised Author: Peter E Shaw. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB Ref "Functional analysis of the Hspassociated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp". Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Takahashi N(1), Hayano T, Suzuki M. Author information: (1)Corporate Research and Development Laboratory, Ioa Nenryo, Kogya K.K., Saitama, by: The cis/trans isomerisation of a peptidyl-prolyl bond leads to a different propagation direction of the polypeptide backbone in each isomer. "The cis/trans isomerisation at the peptide bond N-terminal to proline resembles a molecular switch with the following characteristics: 1. There are two switch positions, other positions are unstable 2.