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1. Peptidyl-prolyl Cis/Trans Isomerases and Cis/Trans Isomerisation of Peptidyl-prolyl Bonds - JenaLib
IMB Jena Image Library Home Page QuickSearch: go by PDB,NDB,UniProt,PROSITE Code or Search Term s collapse expand Home Contact Hetero DB Site DB GO2PDB Genus/Species Classification Trees Entry Lists Search Peptidyl prolyl Cis/Trans Isomerases and Cis/Trans Isomerisation of Peptidyl prolyl Bonds General Aspects In protein structures the planar peptide bond occurs predominantly in the trans conformation Ramachandran & Sasisekharan, Adv. The cis/trans isomerisation of the peptide bonds on the N terminal side of proline residues plays an important role in the folding process of a protein Schmid & Baldwin, Proc. The isomerisation of the peptide bond preceeding proline residues may limit the refolding rate of proteins in vitro and in vivo Brandts et al. A class of enzymes,
http://www.imb-jena.de/ImgLibDoc/cispep/proline/IMAGE_CISPEP1.html
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2. PEPTIDYL PROLYL CIS-TRANS ISOMERASES - Patent EP1117806
SEARCH: Submit GO TO ADVANCED SEARCH LOGIN: Login Create Free Account HOME SEARCH PATENTS CHEMICAL SEARCH DATA SERVICES HELP PEPTIDYL PROLYL CIS TRANS ISOMERASES European Patent Application EP1117806 Kind Code: A1 Abstract not available for EP1117806 Abstract of corresponding document: WO0018934 The present invention provides a method for producing a secretable polypeptide in a host cell, comprising overexpressing a peptidyl prolyl cis trans isomerase in the host cell, thereby increasing the yield of the secreted polypeptide, and a novel peptidyl prolyl cis trans isomerase from A. DK Application Number: EP19990969744 Publication Date: 07/25/2001 Filing Date: 09/30/1999 View Patent Images: Download PDF EP1117806 pdf PDF help Export Citation: Click for automatic biblio
http://www.freepatentsonline.com/EP1117806.html
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3. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical prote
Sign on SAO/NASA ADS General Science Abstract Service . Find Similar Abstracts with default settings below . Electronic Refereed Journal Article HTML . References in the article . Citations to the Article 25 Citation History . Refereed Citations to the Article . Reads History . 476 478 1989 . Nature Homepage Publication Date: 02/1989 Origin: NATURE Abstract Copyright: c 1989: Nature DOI: 10.1038/337476a0 Bibliographic Code: 1989Natur.337..476F Abstract The enzyme peptidyl prolyl cis trans isomerase PPIase was recently discovered in mammalian tissues and purified from porcine kidney 1. The results indicate that this enzyme is probably identical to cyclophilin, a recently discovered mammalian protein which binds tightly to cyclosporin A CsA . The first 38 amino acid re
http://adsabs.harvard.edu/abs/1989Natur.337..476F
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4. GO term: peptidyl-prolyl cis-trans isomerase activity
peptidyl prolyl cis trans isomerase activity 16 genes directly annotated to this term Locus Evidence Annotation Method Reference Assigned By CPR1/YDR155C IDA: Inferred from Direct Assay Assigned on 2002 10 10 manually curated Haendler B, et al. Gene 83 1 :39 46 SGD Papers Entry Pubmed Entry SGD IEA: Inferred from Electronic Annotation with EBI:IPR020892, EBI:IPR002130 Last Updated 2009 11 20 computational DDB, et al. SGD Papers Entry Reference full text UniProtKB IEA: Inferred from Electronic Annotation with IUBMB:5.2.1.8 Last Updated 2009 11 20 computational GOA curators and MGI curators 2001 Gene Ontology annotation based on Enzyme Commission mapping. SGD Papers Entry Reference full text UniProtKB IEA: Inferred from Electronic Annotation with EBI:KW 0697 Last Updat
http://www.yeastgenome.org/cgi-bin/GO/goTerm.pl?goid=3755
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5. GO term: peptidyl-prolyl cis-trans isomerase activity
Genes Annotated with this Term Help This diagram shows the local area of the Gene Ontology and the numbers of yeast genes annotated to each term in the diagram. Genes Annotated with this Term Help This table summarizes the number of genes that have been directly annotated to the term peptidyl prolyl cis trans isomerase activity or to its variants containing one or more qualifiers NOT, contributes to, or colocalizes with in the manually curated set and any annotations made from high throughput experiments or computational analysis. In total, 12 Candida albicans genes have been directly annotated to the term peptidyl prolyl cis trans isomerase activity. Number of Genes Annotated GO Term Download all data Manually Curated GO Annotations 3 peptidyl prolyl cis trans isome
http://www.candidagenome.org/cgi-bin/GO/go.pl?goid=3755
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6. Periplasmic peptidyl prolyl cis-trans isomerases a... [J Bacteriol. 2005] - PubMed result
NCBI Logo Resources All Resources Literature o Bookshelf o Journals Database o MeSH Database o PubMed o PubMed Central o All Literature Resources... DNA & RNA o BankIt o BLAST o BLAST Stand alone o GenBank o Genome Workbench o Influenza Virus o Nucleotide Database o PopSet o Reference Sequence RefSeq o Sequence Read Archive SRA o Trace Archive o All DNA & RNA Resources... Proteins o BLAST o BLAST Stand alone o BLAST Link BLink o CD Search o GenBank o ProSplign o Protein o Protein Clusters o Reference Sequence RefSeq o All Proteins Resources... Sequence Analysis o BLAST o BLAST Stand alone o BLAST Link BLink o GenBank o Genome Workbench o Influenza Virus o Primer BLAST o ProSplign o Splign o All Sequence Analysis Resources... Genes & Expression o GenBank o Gene o Gene
http://www.ncbi.nlm.nih.gov/pubmed/16267292
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7. IngentaConnect Changes in peptidyl-prolyl cis/trans isomerase activity and fk506...
#Latest TOC RSS Feed for 4 Recent Issues RSS Feed for 4 BibText Export for 4 EndNote Export IngentaConnect Home About Ingenta Ingenta Labs Ingenta Blog Help Check our FAQs Or contact us to report problems with: Subscription access Article delivery Registration Library administrator tasks Other problems For Publishers down arrow Why go online? Beyond Print: enhancing your service Access and authentication Article purchasing Managing your publications Usage statistics Reference linking services Branding opportunities Keeping in touch Contact us For Researchers down arrow For Authors About IngentaConnect Search and browse Publications available Accessing articles Managing your account Creating marked lists Creating Saved searches Receiving email alerts Subscribing to RS
http://www.ingentaconnect.com/content/els/03064522/2003/00000120/00000004/art004
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8. Peptidyl-Prolyl cis-trans Isomerase Improves the Efficiency of Protein Disulfide
Sign on SAO/NASA ADS Physics Abstract Service · Find Similar Abstracts with default settings below · Electronic On line Article HTML · Full Printable Article PDF/Postscript · Reads History · · Translate This Page Title: Peptidyl Prolyl cis trans Isomerase Improves the Efficiency of Protein Disulfide Isomerase as a Catalyst of Protein Folding Authors: Schonbrunner, E. In particular, the efficiency of protein disulfide isomerase EC 5.3.4.1 as a catalyst of disulfide bond formation in the course of oxidative folding is markedly improved when peptidyl prolyl cis trans isomerase is present simultaneously. The interdependence of the two enzymatic activities detected during in vitro folding experiments could be of importance for the de novo folding and disulfide bond format
http://adsabs.harvard.edu/abs/1992PNAS...89.4510S
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9. Pin1At Encoding a Peptidyl-Prolyl cis/trans Isomerase Regulates Flo...
Please, select a folder to save the following article article name will be there New Folder|Rename|Delete Save Cancel Article has been saved successfully. Epub ahead of print PMID: 17851766 PubMed as supplied by publisher Please, choose a category Life Science Bioinformatics Cancer Biology Development Drug Discovery Genetics Immunology Mol / Cell Biology Neuroscience Other Life Sciences Clinical Medicine Cardiology Endocrinology GI / Hepatology Infectious Diseases Neurology Oncology Pulm / Critical Care Renal / Urology Other Clinical Submit Cancel The article has been promoted. Go to this article Close This article is already in the system. Saved Articles Please, login: Go or register to use this function. We show that an Arabidopsis PIN1 type parvulin 1, Pin1At, con
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11. IngentaConnect X-ray structure of peptidyl-prolyl cistrans isomerase A from Myco...
#Latest TOC RSS Feed for 20 Recent Issues RSS Feed for 20 BibText Export for 20 EndNote Export IngentaConnect Home About Ingenta Ingenta Labs Ingenta Blog Help Check our FAQs Or contact us to report problems with: Subscription access Article delivery Registration Library administrator tasks Other problems For Publishers down arrow Why go online? Beyond Print: enhancing your service Access and authentication Article purchasing Managing your publications Usage statistics Reference linking services Branding opportunities Keeping in touch Contact us For Researchers down arrow For Authors About IngentaConnect Search and browse Publications available Accessing articles Managing your account Creating marked lists Creating Saved searches Receiving email alerts Subscribing to
http://www.ingentaconnect.com/content/bsc/ejb/2004/00000271/00000020/art00014
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12. Peptidyl-prolyl cis-trans isomerase - Legionella quateirensis
Peptidyl prolyl cis trans isomerase Legionella quateirensis Skip Header › UniProtKB Downloads · Contact · Documentation/Help Search in Protein Knowledgebase UniProtKB Sequence Clusters UniRef Sequence Archive UniParc Literature citations Taxonomy Keywords Subcellular locations News Documents User manual FAQ Help Query Fields » ID Mapping Retrieve Align Blast Search Sequence tr|O32835|O32835 9GAMM Peptidyl prolyl cis trans isomerase OS Legionella quateirensis GN mip PE 3 SV 1 MKMKLVTAAVLGLAMSTAMATDATSLPTDKDKLSYSIGADLGKNFKNQGIDVNPEALAKG MQDGMSGAQLILTEQQMKDVLNKFQKDLMAKRTSEFNKKAEENKSKGEAFLTENKSKTGV VVLPSGLQYKIIDAGTGAKPGKSDTVTVEYTGRLIDGTVFDSTEKTGKPATFQVSQVIPG WTEALQLMPAGSTWEIYVPASLAYGPRSVGGPIGPNETLIFKIHLISVKKSAS Blast Clear « Options Options » Blast tips You can enter: •
http://www.uniprot.org/uniprot/O32835?tab=batch
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13. RCSB PDB : Structure Summary for 1PIN - PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
#RCSB PDB Latest Released Structures RCSB Full Text or PDB ID Search RCSB Author Search POP OUT | NMR Validation Server BioSync Beamline Related Tools Move Section Search Hide Advanced Search Latest Release Latest Publications Sequence Search Chemical Components Unreleased Entries Browse Database Histograms Explorer: Last Structure: 1PIN Move Section Tools Hide File Downloads FTP Services File Formats Services: RESTful | Methods Geometry Links PIN1 PEPTIDYL PROLYL CIS TRANS ISOMERASE FROM HOMO SAPIENS DOI:10.2210/pdb1pin/pdb 1PIN Display Files close FASTA Sequence PDB File PDB File Header mmCIF File mmCIF File Header PDBML/XML File PDBML/XML File Header Download Files close FASTA Sequence PDB File Text PDB File gz mmCIF File mmCIF File gz PDBML/XML File PDBML/XML Fil
http://www.pdb.org/pdb/explore.do?structureId=1pin
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15. Human protein: IPI00419585 * 18012 Da * PPIA Peptidyl-prolyl cis-trans isomerase A - Bioinformatic Harvester @ KIT
Human protein: IPI00419585 18012 Da PPIA Peptidyl prolyl cis trans isomerase A Liebel Lab KIT Bioinformatic Harvester logo PPIA Peptidyl prolyl cis trans isomerase A Length: 165 AS MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD CGQLE Linkouts to other data resources: BioCompare Entrez PolyMeta GeneCard imaGenes GenomeBrowser Google Scholar Mitocheck AceView BLAST CDD ensEMBL EntrezGene GoPubMed H Inv IHOP Localisation MINT OMIM ProteinWiki SMART UNIPROT STRING crosslinks top of page : gene&Cmd ShowDetailView&Ter mToSearch 5478 AceView BLAST CDD ensEMBL EntrezGene GoPubMed H Inv IHOP Localisation MINT OMIM ProteinWiki SMART UNIPROT STRING crosslinks top
http://harvester.fzk.de/harvester/human/IPI00419/IPI00419585.htm
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16. Peptidyl-prolyl isomerases: a new twist to transcription
EMBO reports Advertisement EMBO reports SEARCH search EMBO reports My Account Submit manuscript Subscribe Register Help Journal home Aims and scope Current issue editorial science & society reviews scientific reports Advance Online Publication Web Focuses Archive: Browse by issue Browse by subject Browse by article type Press releases Authors and referees Guide for authors Submit Manuscript Guide for referees Editors and editorial board Contact editorial office Customer Services Subscribe Order sample copy Purchase articles Reprints and permissions Contact NPG Advertising concept EMBO reports 3, 6, 521–526 2002 doi:10.1093/embo reports/kvf118 Peptidyl prolyl isomerases: a new twist to transcription Peter E. Hence a role for PPIs in the folding of newly synthesised pr
http://www.nature.com/embor/journal/v3/n6/full/embor140.html
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17. Peptidyl-prolyl cis-trans isomerase A - Homo sapiens (Human)
partial Ref.9 Modified residue 21 1 Phosphoserine By similarity Modified residue 28 1 N6 acetyllysine Ref.16 Modified residue 44 1 N6 acetyllysine Ref.16 Modified residue 49 1 N6 acetyllysine Ref.16 Modified residue 76 1 N6 acetyllysine Ref.16 Modified residue 82 1 N6 acetyllysine Ref.16 Modified residue 125 1 N6 acetyllysine Ref.16 Ref.13 Modified residue 131 1 N6 acetyllysine Ref.16 Modified residue 157 1 Phosphothreonine Ref.12 Cross link 28 Glycyl lysine isopeptide Lys Gly interchain with G Cter in ubiquitin Ref.14 Experimental info Mutagenesis 121 1 W ? A: 200 fold decrease of sensitivity to CsA. Beta strand 5 – 12 8 Beta strand 15 – 24 10 Turn 26 – 28 3 Helix 30 – 41 12 Turn 42 – 44 3 Beta strand 55 – 57 3 Turn 58 – 60 3 Beta strand 61 – 64 4 Turn 67 – 69 3 Bet
http://www.uniprot.org/uniprot/P62937
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18. Inhibition of peptidyl-prolyl cis/trans isomerase activity by substrate analog structures: thioxo tetrapeptide-4-nitroanilides -
Cart Home Browse the Journal List of Issues Current Issue Just Accepted Manuscripts Most Read Articles Most Cited Articles Sample Issue Author Index Cover Art Gallery Articles ASAP Current Issue Submission & Review Info for Authors & Reviewers Submit a Manuscript or Review Ethical Guidelines Copyright & Permissions/Rightslink ACS Author & Reviewer Resource Center Subscriptions About the Journal About the Journal Editors Editor Profile Masthead PDF Editorial Advisory Board PDF Advertising Prev. Fischer Close Menu JOURNALS A Accounts of Chemical Research ACS Applied Materials & Interfaces ACS Chemical Biology ACS Chemical Neuroscience ACS Medicinal Chemistry Letters ACS Nano Analytical Chemistry I&EC Analytical Edition B Biochemistry Bioconjugate Chemistry Biomacromole
http://pubs.acs.org/doi/abs/10.1021/bi00040a012
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19. FKBP-type 22 kDa peptidyl-prolyl cis-trans isomerase - Escherichia coli (strain K12)
#home UniProtKB RDF RSS Skip Header › UniProtKB Downloads · Contact · Documentation/Help Search Blast Align Retrieve ID Mapping Search in Protein Knowledgebase UniProtKB Query Search Fields » Search Blast Align Retrieve ID Mapping Sequence Submit Blast Clear « Options Options » Blast tips You can enter: • a protein or nucleotide sequence • a valid UniProt identifier, for example: P00750 or A4 HUMAN or UPI0000000001 More... Search Blast Align Retrieve ID Mapping Sequences Submit Align Clear ClustalW tips Enter either: • two or more sequences in FASTA format • two or more UniProt identifiers, for example: P00750 P00750 2 UniRef100 P00750 More... Search Blast Align Retrieve ID Mapping Identifiers Submit Retrieve Clear or Batch retrieval tips Enter or upload a list of Un
http://www.uniprot.org/uniprot/P0A9L3
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20. Flipkart.com: Peptidyl-prolyl Cis/trans Isomerases: Andrezj Galat, Sylvie Riviere,: Books: Sylvie Riviere
HomeMy AccountShopping Cart 0 items Contact UsHelpLogin/Signup Search for Books: Search Buy Books in India The book store at your door! Peptidyl prolyl Cis/trans Isomerases protein Profile , Andrezj Galat, Sylvie Riviere,, 0198502885 Look Inside This Book Peptidyl prolyl Cis/trans Isomerases protein Profile Paperback 1999 01 28 by Andrezj Galat , Sylvie Riviere , Write a Review List Price: Rs. See Details OR Buy This Item Book: Peptidyl prolyl Cis/trans Isomerases protein Profile Peptidyl prolyl cist/trans isomerases PPIases are a family of proteins that are present in a wide range of species. 9093 Details of Book: Peptidyl prolyl Cis/trans Isomerases protein Profile Book: Peptidyl prolyl Cis/trans Isomerases protein Profile Author: Andrezj Galat, Sylvie Riviere, ISB
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