Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity. - Wikidata - awgldk - TriplyDB

Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.

Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.

http://www.wikidata.org/entity/Q33202132

about

Siderophore-based iron acquisition and pathogen control Beware of proteins bearing gifts: protein antibiotics that use iron as a Trojan horse The bacterial chemical repertoire mediates metabolic exchange within gut microbiomes The 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.Isolation and characterization of two members of the siderophore-microcin family, microcins M and H47 Advances in iron chelation: an update.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Microcins in action: amazing defence strategies of Enterobacteria.Microcin e492 amyloid formation is retarded by posttranslational modification.Total (bio)synthesis: strategies of nature and of chemists.Bactericidal activity of both secreted and nonsecreted microcin E492 requires the mannose permease.Beyond iron: non-classical biological functions of bacterial siderophores Genome-Wide Screening Identifies Six Genes That Are Associated with Susceptibility to Escherichia coli Microcin PDI Natural products as mediators of disease.Biosynthetic tailoring of microcin E492m: post-translational modification affords an antibacterial siderophore-peptide conjugate.Iron metabolism at the host pathogen interface: lipocalin 2 and the pathogen-associated iroA gene cluster.Follow the leader: the use of leader peptides to guide natural product biosynthesis.How nature morphs peptide scaffolds into antibiotics Is drug release necessary for antimicrobial activity of siderophore-drug conjugates? Syntheses and biological studies of the naturally occurring salmycin "Trojan Horse" antibiotics and synthetic desferridanoxamine-antibiotic conjugates Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds.Microcin PDI regulation and proteolytic cleavage are unique among known microcins.Microbial manipulation of the amyloid fold.Catechol-based biomimetic functional materials.Siderophore-dependent iron uptake systems as gates for antibiotic Trojan horse strategies against Pseudomonas aeruginosa.Fold modulating function: bacterial toxins to functional amyloids.Chemical and Biological Aspects of Nutritional Immunity - Perspectives for New Anti-infectives Targeting Iron Uptake Systems.Lasso peptide, a highly stable structure and designable multifunctional backbone.Siderophores as molecular tools in medical and environmental applications.Biosynthetic considerations of triscatechol siderophores framed on serine and threonine macrolactone scaffolds.Bifunctional antimicrobial conjugates and hybrid antimicrobials.Whole-Genome Sequence of the Microcin E492-Producing Strain Klebsiella pneumoniae RYC492.Catechol siderophores repress the pyochelin pathway and activate the enterobactin pathway in Pseudomonas aeruginosa: an opportunity for siderophore-antibiotic conjugates development.The production in vivo of microcin E492 with antibacterial activity depends on salmochelin and EntF.Sideromycins: tools and antibiotics Identification of Key Amino Acid Residues Modulating Intracellular and In vitro Microcin E492 Amyloid Formation Cooperative uptake of microcin E492 by receptors FepA, Fiu, and Cir and inhibition by the siderophore enterochelin and its dimeric and trimeric hydrolysis products.Antibiotics and specialized metabolites from the human microbiota.Enterobactin-mediated delivery of β-lactam antibiotics enhances antibacterial activity against pathogenic Escherichia coli.In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes.

P2860

Q24681774-8AD4D9C9-CF19-48ED-AD94-13BACDBA70A8 Q26863492-648C6FE9-7774-4C50-8C72-2BE2704AB03F Q27000963-69F2EEA5-5E7E-4F76-9F25-C0AC597C6279 Q31165543-226BF466-5E0F-4CB2-ACAF-DD1B2DFC35D5 Q33291487-8164AE46-3737-4826-B2CB-1C798B05F1B7 Q33514594-9E9EC29E-7CFA-44CD-89A1-4ADFBF8CCC4C Q34174307-3FE40C58-8BA2-41AC-8D76-5CB5DA593D09 Q34312732-96E7ECD0-6F23-43D3-8BC4-CBD61D1C1CC7 Q34486998-DC301661-BAE8-4E9D-B7CF-89E8F8C1F0A6 Q34803136-89F5D721-2050-4A68-976C-6BFD1DA31B69 Q35028522-56A7F3FD-3261-46DE-94C6-A575E205CD4F Q35130137-6221BE66-7DF7-4756-A5BF-FF002664AB26 Q35220353-8CE531C3-3F61-4F2B-8604-F4CCB179099B Q35713362-F95A41B5-01E1-4D53-886D-F34710E41975 Q36200942-02C44E1C-46FA-4DD9-B24F-B52D838CAD07 Q36848822-3F8A6733-CAC6-4971-910D-D06F9721B28D Q36917365-D7D4342D-28AD-4C66-937C-09BC1D44D77F Q37237843-9B7EE8DA-D3A7-4265-BE86-8570F8BA5FD5 Q37341890-C92D9DDF-AE43-45CC-84EB-74FA37AE3407 Q37394682-FF5C6CCD-F106-4935-9256-ACFFD1A8695F Q37566506-B34B4193-9248-4D55-9435-D86E8D3C4DFF Q37644356-B854A0D0-2EEA-4BBE-9C0B-1256B893F937 Q38056340-CDF51D9A-673D-4DE1-899D-D81429429558 Q38062517-8304ABB4-18C5-4916-9B4E-282F46551ADF Q38183671-3F25548C-41BA-4AB4-818F-7EF90CA69D2E Q38241187-1F75C614-B2BB-413E-AEB6-AE38E70E335C Q38691254-CFA37114-B38F-4B5C-BD99-C44962AD89BC Q38807411-F0ABDB49-A070-40C7-A2FC-43A6A9C7C325 Q38919129-0B6BDA4E-1269-4D95-966C-08122DB177C6 Q39359232-883D7B72-018E-4E4E-9B17-28548975323C Q40203926-7A9F425A-0EFE-4AB6-8FC3-6B0035A7ED51 Q40602029-A60072AA-E8A9-409F-AFF7-00EACE9DA10F Q40850140-F1704FD8-B19B-45AC-9D11-4724C2A56A93 Q41340306-427B317B-32A9-48AE-B8E4-814A81F7DFB8 Q41440537-81A043BC-94FF-45B1-BF13-6A37CF69A758 Q41827272-B03DB787-7B6F-4D26-A172-2E849B5F0BE6 Q41891980-9368220B-2E5F-49AE-98A3-1766828E718C Q41987403-9852D63D-0222-4075-B5B7-6E6F727AE2AE Q42257669-E386EC20-9ACB-47A5-92BB-037BEE5D18AD Q42532144-9D99390A-2156-4E05-9FBF-FE74377A7DC6

P2860

Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.

http://www.wikidata.org/entity/Q33202132

description

2004 nî lūn-bûn

@nan

2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Siderophore peptide, a new typ ...... peptide with potent activity.

@ast

Siderophore peptide, a new typ ...... peptide with potent activity.

@en

type

label

Siderophore peptide, a new typ ...... peptide with potent activity.

@ast

Siderophore peptide, a new typ ...... peptide with potent activity.

@en

prefLabel

Siderophore peptide, a new typ ...... peptide with potent activity.

@ast

Siderophore peptide, a new typ ...... peptide with potent activity.

@en

P1433

Q33202132-7F23EA6D-2217-42B1-AE43-5DC21C8DF508

P1476

Q33202132-CFEC3CB5-4A17-45D7-B4DC-FF53F4FFC10C

P2093

Q33202132-1A55F633-52F3-4699-B554-BE884F3E193A

Q33202132-428AF36C-BED0-46C2-A1A9-92AAAC48D054

Q33202132-50A80CB1-1E9C-4767-8518-CDA176ED21ED

Q33202132-64E8E8B5-AB20-4F6A-A97E-215A9896D7E4

Q33202132-72C01595-8861-492E-B106-CEEA1A21C187

Q33202132-B46499A0-186F-4884-BAE0-26C921D560CF

Q33202132-D03552D4-7728-4ABB-B623-3BC4B9536DFC

Q33202132-D9633200-5048-4AA9-8D80-AB3264DE6A04

P2860

Q33202132-089193C2-E8A5-4564-A87F-B87718E7954A

Q33202132-116C5045-FF35-499C-8611-1DC83CA8230E

Q33202132-1CFEEA0D-F2C8-4F25-9D2A-EB9B88E4C076

Q33202132-24358DF6-EB20-406D-8A93-C4CEF57023FF

Q33202132-2ED54FB5-BAA0-49DA-B081-662AD845C60A

Q33202132-3375A310-3567-42D4-B172-2157DA8AC818

Q33202132-3C49FF41-38CD-49BF-BE52-F91A07987F5F

Q33202132-630C6E04-E1DF-4E14-8083-51AA6244B566

Q33202132-714E9CCA-452F-45C9-8E50-351615585598

Q33202132-8184A316-BA99-431B-8B11-EDADF0A1ED13

P304

Q33202132-ECCD7B86-5762-482D-BFA0-E787246506D4

P31

Q33202132-F627406F-5D74-41F6-AE3B-24E9C0DC1B72

P356

Q33202132-47E35EFD-19AC-4CEC-8EA5-83694320C291

P407

Q33202132-AE9D39DE-0CA7-4A3E-92D7-E894DEA60220

P433

Q33202132-3C6B32B3-0439-49B0-A23C-AC510F06C380

P478

Q33202132-C33B63F2-611E-4F0B-8E4C-60C08B066AEC

P50

Q33202132-1C26F8BC-F3AB-4F2D-9059-4CA1B806C0F0

Q33202132-A073ADE6-0246-458B-9811-05DF33BA0F76

Q33202132-ECF64F48-1EC5-46E5-AE87-8C76B12DBB9F

P577

Q33202132-AF4D8428-3F4D-4C5F-BDF6-D10DFE1BCBD5

P698

Q33202132-647E15E0-485F-44F9-ADBC-D70B946A60F0

P356

P1433

Journal of Biological Chemistry

P1476

Siderophore peptide, a new typ ...... peptide with potent activity.

@en

P2093

Alain Blond

http://www.w3.org/2001/XMLSchema#string

Christophe Goulard

http://www.w3.org/2001/XMLSchema#string

Jean Peduzzi

http://www.w3.org/2001/XMLSchema#string

Jean-Claude Tabet

http://www.w3.org/2001/XMLSchema#string

Lionel Dubost

http://www.w3.org/2001/XMLSchema#string

Nicolas Birlirakis

http://www.w3.org/2001/XMLSchema#string

Robert Thai

http://www.w3.org/2001/XMLSchema#string

Xavier Thomas

http://www.w3.org/2001/XMLSchema#string

P2860

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

Proposal for a common nomenclature for sequence ions in mass spectra of peptides

Enterobactin, an iron transport compound from Salmonella typhimurium

Focus on modified microcins: structural features and mechanisms of action.

Microcin E492 is an unmodified peptide related in structure to colicin V

Microcin E492 antibacterial activity: evidence for a TonB-dependent inner membrane permeabilization on Escherichia coli.

Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA.

Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN

P304

28233-28242

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M400228200

http://www.w3.org/2001/XMLSchema#string

P407

P433

27

http://www.w3.org/2001/XMLSchema#string

P478

279

http://www.w3.org/2001/XMLSchema#string

P50

Delphine Destoumieux-Garzón

Sylvie Rebuffat

P577

2004-04-21T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

15102848

http://www.w3.org/2001/XMLSchema#string