NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein
about
Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation.The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in HominidaeParvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineageSmall family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical researchCrystal Structure of Escherichia coli Rnk, a New RNA Polymerase-Interacting ProteinSolution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulinsThe prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activityStructure and Dynamics of the First Archaeal Parvulin Reveal a New Functionally Important Loop in Parvulin-type Prolyl IsomerasesIsolation and proteomic characterization of human Parvulin-associating preribosomal ribonucleoprotein complexesSolution structural analysis of the single-domain parvulin TbPin1Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.Identification and characterization of peptides that bind the PPIase domain of Parvulin17.Dimeric Structure of the Bacterial Extracellular Foldase PrsA.Single-domain parvulins constitute a specific marker for recently proposed deep-branching archaeal subgroupsHuman DNA-binding peptidyl-prolyl cis/trans isomerase Par14 is cell cycle dependently expressed and associates with chromatin in vivo.Roles of Prolyl Isomerases in RNA-Mediated Gene ExpressionNmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.Comparative analysis of enzyme activities and mRNA levels of peptidyl prolyl cis/trans isomerases in various organs of wild type and Pin1-/- mice.Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases.Molecular and biochemical characterization of the parvulin-type PPIases in Lotus japonicus.Peptide binding induces large scale changes in inter-domain mobility in human Pin1.Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis.
P2860
Q21263004-584CF3AD-6099-459F-B78E-9F76FF60D387Q24293963-2DDE4348-3A91-4A85-B8E1-89E67D050B4AQ24315973-F7770312-7FBF-40EE-BAA6-1446704A6074Q24651965-BD8A6560-336E-4B51-91B6-22D360245DC8Q27651883-6601DC81-98E7-4EA0-90E2-64E73FE29F42Q27654271-D69AA314-55EA-48D0-9F94-1295BA879CFBQ27658010-0B75CD3D-B9C0-452F-A3BB-6B3B5294F7D0Q27666214-1E8FB9A0-7E26-44CD-80F0-19440F5D651CQ28215155-05A992EB-9105-47AD-988A-3E9D2971ECE4Q28482188-775D8AB0-D4C9-4F0A-AD78-BE1DBC5B7517Q30316581-8CD014A2-5A0C-4697-9A48-0FEC1086BC37Q34675952-C7EB1594-4F06-4050-8671-660E5EB30681Q35055492-8EEB3E50-A530-416F-B5FE-027363649B84Q35486181-DAEC7AE3-2C03-4738-AB95-0960711AB868Q35553939-3DA00F36-4C90-425F-BCC5-E087DFCAA3CBQ35834035-93CDE052-3526-4957-B530-5897D169D3F3Q36062775-8BBE35D7-687D-46E4-8969-E7D4217823CFQ42495304-23DE75D3-4096-4B4B-9C9B-9B20353112C8Q43095107-179E6780-0F22-403B-AA14-FFC66980CB7AQ46031560-DD1E9FFB-B606-4AD6-AAC1-DC7FB8450607Q47986427-ABD76C54-A0D6-483C-B590-C7917C7C0A50Q51026793-0DE074BC-E51C-457B-94AA-9FCF1607B585
P2860
NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
NMR solution structure of hPar ...... t functionality of the protein
@ast
NMR solution structure of hPar ...... t functionality of the protein
@en
NMR solution structure of hPar ...... t functionality of the protein
@nl
type
label
NMR solution structure of hPar ...... t functionality of the protein
@ast
NMR solution structure of hPar ...... t functionality of the protein
@en
NMR solution structure of hPar ...... t functionality of the protein
@nl
prefLabel
NMR solution structure of hPar ...... t functionality of the protein
@ast
NMR solution structure of hPar ...... t functionality of the protein
@en
NMR solution structure of hPar ...... t functionality of the protein
@nl
P2093
P3181
P356
P1476
NMR solution structure of hPar ...... t functionality of the protein
@en
P2093
P304
P3181
P356
10.1006/JMBI.2000.4013
P407
P50
P577
2000-08-01T00:00:00Z