Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity.
about
Structure, Bioactivity, and Resistance Mechanism of Streptomonomicin, an Unusual Lasso Peptide from an Understudied Halophilic ActinomycetePrecursor-centric genome-mining approach for lasso peptide discoveryXanthomonins I-III: a new class of lasso peptides with a seven-residue macrolactam ringThe iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11-Pro16 beta-hairpin region in the recognition mechanism.Insight into siderophore-carrying peptide biosynthesis: enterobactin is a precursor for microcin E492 posttranslational modification.Structure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymeraseStructures of naturally occurring circular proteins from bacteria.The front line of enteric host defense against unwelcome intrusion of harmful microorganisms: mucins, antimicrobial peptides, and microbiotaIdentification and characterization of leucocyclicin Q, a novel cyclic bacteriocin produced by Leuconostoc mesenteroides TK41401.NMR as an effective tool for the structure determination of lasso peptides.Gemmata species: Planctomycetes of medical interest.Synthesis and stabilities of peptide-based [1]rotaxanes: molecular grafting onto lasso peptide scaffolds.Lasso peptides from proteobacteria: Genome mining employing heterologous expression and mass spectrometry.Lasso-inspired peptides with distinct antibacterial mechanisms.
P2860
Q27644318-0CDE229F-E297-48B9-8F89-66AA529E4C57Q27672155-E9624F41-0EAA-4598-A788-536D34971A10Q27688948-CE0CD2C0-4616-4709-B77E-846F0B8F4DF7Q31165543-6263541F-8829-40D3-9E54-932937376815Q33291487-E6A99CB4-6E47-4EB1-9E34-0BC44AFDCB32Q33788522-28ECF8A8-438F-46AB-BFCC-E40E094856ADQ34210698-3E511F7A-A625-4081-8633-9DDCFECB1BF4Q34647328-A8FCF53F-91AB-4AE8-9FE3-12E6A2FD5B95Q35530173-B32C6FC2-DAA5-40C2-93EE-F37EA5C06D3BQ37978834-F0C4A47D-E605-4EA1-88BE-4A98ED776FAEQ38829548-8DF989B3-2B6E-4CFA-9B31-51630FB91B56Q41996691-38A4B13B-006F-4D23-B69B-0584010E36C5Q46224005-4F69481C-8650-4BDF-A063-17F32A3EEFD2Q49995296-12326BD7-C830-4D76-B8E4-F3A7B28234A9
P2860
Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity.
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Thermolysin-linearized microci ...... splays antimicrobial activity.
@ast
Thermolysin-linearized microci ...... splays antimicrobial activity.
@en
type
label
Thermolysin-linearized microci ...... splays antimicrobial activity.
@ast
Thermolysin-linearized microci ...... splays antimicrobial activity.
@en
prefLabel
Thermolysin-linearized microci ...... splays antimicrobial activity.
@ast
Thermolysin-linearized microci ...... splays antimicrobial activity.
@en
P2093
P2860
P1433
P1476
Thermolysin-linearized microci ...... splays antimicrobial activity.
@en
P2093
Alain Blond
Christophe Goulard
Isabelle Ségalas-Milazzo
Jean Peduzzi
Michel Cheminant
P2860
P304
P356
10.1046/J.1432-1033.2002.03340.X
P407
P577
2002-12-01T00:00:00Z