Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK
about
Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrateThe proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complexDnaK as Antibiotic Target: Hot Spot Residues Analysis for Differential Inhibition of the Bacterial Protein in Comparison with the Human HSP70Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity.Discovery of novel interacting partners of PSMD9, a proteasomal chaperone: Role of an Atypical and versatile PDZ-domain motif interaction and identification of putative functional modulesThe mechanism of inhibition of protein synthesis by the proline-rich peptide oncocinOptimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus.Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.Proline-rich antimicrobial peptides targeting protein synthesis.Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition.Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Super Spy variants implicate flexibility in chaperone action.In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria.How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data.Insect-derived short proline-rich and murine cathelicidin-related antimicrobial peptides act synergistically on Gram-negative bacteria in vitro.Immunogenicity and pharmacokinetics of short, proline-rich antimicrobial peptides.Structural Insights into Substrate Recognition and Catalysis in Outer Membrane Protein B (OmpB) by Protein-lysine Methyltransferases from Rickettsia.Ribosomal binding and antibacterial activity of ethylene glycol-bridged apidaecin Api137 and oncocin Onc112 conjugates.BiPPred: Combined sequence- and structure-based prediction of peptide binding to the Hsp70 chaperone BiP.Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE.Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Hsp70/J-protein machinery from Glossina morsitans morsitans, vector of African trypanosomiasisInsect-derived proline-rich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70S ribosome.Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interactionThe β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions.Insect antimicrobial peptides show potentiating functional interactions against Gram-negative bacteria.Optimization of adiponectin-derived peptides for inhibition of cancer cell growth and signaling.Protein polarization driven by nucleoid exclusion of DnaK(HSP70)-substrate complexes.Advantage of a Narrow Spectrum Host Defense (Antimicrobial) Peptide Over a Broad Spectrum Analog in Preclinical Drug DevelopmentSynergy Between Proline-Rich Antimicrobial Peptides and Small Molecule Antibiotics Against Selected Gram-Negative Pathogens and
P2860
Q21090602-D8F7C544-8FD4-4C0F-8D6D-F453626977ECQ27700868-5442E4F0-5398-4C8A-AF1E-3A518E8655C8Q28546662-C59EEBCF-48DF-4FA6-9F90-E3DACB7CD254Q33684457-AE5CC1A4-248D-43F2-BC89-454B0DA5C5DEQ33865030-B0C193C4-B31B-492E-B945-628F0688FC48Q35685002-4573562F-B236-4F6E-B964-089B1249836AQ35762892-B9A0AD4F-53DD-4DA4-AC3D-C0B27849E7CDQ36378270-96E2F6EB-0C13-4807-8267-ED5C4EF6EB0CQ36379116-7FEEE762-95BE-4DB7-A9B3-DC40E4BDA1EBQ36701111-DC1689E1-FFD0-461A-BEDA-3C786AE37479Q37079732-28D0B489-2FD9-4AFF-BB9E-5BF8DF4C70ADQ37542104-36F94890-AA39-46E2-BA76-CEF0EF3B36FDQ37710376-2ECEFEF1-6D02-4494-ABEA-3DE0AC9DAA5CQ38241687-B26A57DE-B093-490A-A033-2FBBA750F1FDQ38356312-FE3606EF-3EAB-4409-93BA-88B5CF3E01D9Q38611961-C8D43C5A-0BCF-4639-B9C4-E7012C9891FBQ38855258-2486C019-E0F4-4E21-9DAB-E2D6A4F78BE9Q38970681-1DF9AF40-C628-4C61-AB41-2FBF804F12F1Q39543220-FF24E6C4-380B-44DD-BC42-2B34E855FCE0Q39608562-A6EC6400-4209-49F1-A3DB-AAC8ED47DFE4Q39692774-80117849-55C0-4C47-9675-DA05DFE360E1Q39715289-C3A052F2-FECA-4B9A-B3A8-161B62E87C79Q41018550-DB17B035-DB75-4D1C-B74C-07B84A3F5343Q41142344-6789B35A-438B-45C5-AE71-19EFE9A02693Q41739821-4AED3274-8307-442D-958C-E698A0F5EFCDQ41933973-41DF3654-F8CE-4EF5-95C4-DEAE7428223CQ47417959-B08D95C0-70D8-4497-95FD-679F9B21A989Q48262474-7BD54A52-4AD3-436A-88AE-C8340BC7557AQ49819851-E6B49E5C-160F-45C6-A285-66E02D7C58CFQ51363895-A4C8E7BC-2B88-45BA-AB6D-8235B8D232DBQ53616040-A5C9E23D-B21B-4920-8B64-4A13BA371F19Q55022646-DD7C9FB8-626B-44C8-BC78-2741CD762ADAQ58728409-5E799D41-9006-447D-BB68-9B8A60E5246BQ58781151-84675B17-7751-4EDE-B9F6-F1B0FC0F5CA9
P2860
Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK
description
2013 nî lūn-bûn
@nan
2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Structural studies on the forw ...... peptides to the chaperone DnaK
@ast
Structural studies on the forw ...... peptides to the chaperone DnaK
@en
Structural studies on the forw ...... peptides to the chaperone DnaK
@nl
type
label
Structural studies on the forw ...... peptides to the chaperone DnaK
@ast
Structural studies on the forw ...... peptides to the chaperone DnaK
@en
Structural studies on the forw ...... peptides to the chaperone DnaK
@nl
prefLabel
Structural studies on the forw ...... peptides to the chaperone DnaK
@ast
Structural studies on the forw ...... peptides to the chaperone DnaK
@en
Structural studies on the forw ...... peptides to the chaperone DnaK
@nl
P2093
P1476
Structural studies on the forw ...... peptides to the chaperone DnaK
@en
P2093
Björn Kieslich
Daniel Knappe
Michael Zahn
Nicole Berthold
Ralf Hoffmann
P304
P356
10.1016/J.JMB.2013.03.041
P407
P577
2013-07-24T00:00:00Z