Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S. - Wikidata - wikimedia - TriplyDB

Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S.

Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S.

http://www.wikidata.org/entity/Q39994987

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HUMAN MICROBIOTA. Small molecules from the human microbiota Structural and functional insight into an unexpectedly selective N-methyltransferase involved in plantazolicin biosynthesis Synthetic biology to access and expand nature's chemical diversity A large scale prediction of bacteriocin gene blocks suggests a wide functional spectrum for bacteriocins Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family Plantazolicin, a novel microcin B17/streptolysin S-like natural product from Bacillus amyloliquefaciens FZB42.Clostridiolysin S, a post-translationally modified biotoxin from Clostridium botulinum.Role of catabolite control protein A in the regulation of intermedilysin production by Streptococcus intermedius.Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates Linking chemistry and genetics in the growing cyanobactin natural products family Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase.Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.Structure determination and interception of biosynthetic intermediates for the plantazolicin class of highly discriminating antibiotics.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Identification of an Auxiliary Leader Peptide-Binding Protein Required for Azoline Formation in Ribosomal Natural Products.Real-time PCR assay to differentiate Listeriolysin S-positive and -negative strains of Listeria monocytogenes.Structure of microcin B-like compounds produced by Pseudomonas syringae and species specificity of their antibacterial action.Photochemical cleavage of leader peptides.Expansion of type II CAAX proteases reveals evolutionary origin of γ-secretase subunit APH-1 Design and evaluation of a peptide-based immunotoxin for breast cancer therapeutics.Identification of the minimal cytolytic unit for streptolysin S and an expansion of the toxin family.The genomic landscape of ribosomal peptides containing thiazole and oxazole heterocycles.A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.Streptolysin S Promotes Programmed Cell Death and Enhances Inflammatory Signaling in Epithelial Keratinocytes during Group A Streptococcus Infection.Insights into the mechanism of peptide cyclodehydrations achieved through the chemoenzymatic generation of amide derivatives.Severe soft tissue infection caused by a non-beta-hemolytic Streptococcus pyogenes strain harboring a premature stop mutation in the sagC gene.Engineering unnatural variants of plantazolicin through codon reprogramming.Follow the leader: the use of leader peptides to guide natural product biosynthesis.Ribosomally synthesized and post-translationally modified peptide natural products: new insights into the role of leader and core peptides during biosynthesis.Implementation of a Permeable Membrane Insert-based Infection System to Study the Effects of Secreted Bacterial Toxins on Mammalian Host Cells Streptolysin S-like virulence factors: the continuing sagA.Orchestration of enzymatic processing by thiazole/oxazole-modified microcin dehydrogenases.Listeriolysin S Is a Streptolysin S-Like Virulence Factor That Targets Exclusively Prokaryotic Cells In Vivo.Streptococcal toxins: role in pathogenesis and disease.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.Unique post-translational oxime formation in the biosynthesis of the azolemycin complex of novel ribosomal peptides from Streptomyces sp. FXJ1.264 In Vitro Biosynthesis and Substrate Tolerance of the Plantazolicin Family of Natural Products.A major portion of DNA gyrase inhibitor microcin B17 undergoes an N,O-peptidyl shift during synthesis.Marine molecular machines: heterocyclization in cyanobactin biosynthesis.Novel twin streptolysin S-like peptides encoded in the sag operon homologue of beta-hemolytic Streptococcus anginosus

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P2860

Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S.

http://www.wikidata.org/entity/Q39994987

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

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2009年學術文章

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2009年學術文章

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2009年學術文章

@zh-hant

name

Structural and functional diss ...... tide cytotoxin streptolysin S.

@en

Structural and functional diss ...... tide cytotoxin streptolysin S.

@nl

type

label

Structural and functional diss ...... tide cytotoxin streptolysin S.

@en

Structural and functional diss ...... tide cytotoxin streptolysin S.

@nl

prefLabel

Structural and functional diss ...... tide cytotoxin streptolysin S.

@en

Structural and functional diss ...... tide cytotoxin streptolysin S.

@nl

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Journal of Biological Chemistry

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Structural and functional diss ...... tide cytotoxin streptolysin S.

@en

P2093

Andrew L Markley

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Jack E Dixon

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Joyce D Limm

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Shaun W Lee

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P2860

Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella

Role of the microcin B17 propeptide in substrate recognition: solution structure and mutational analysis of McbA1-26

OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI. 3. THE RELATIONSHIP OF THE CELL-BOUND HOMOLYSIN TO STREPTOLYSIN S

Identification of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease.

Listeriolysin S, a novel peptide haemolysin associated with a subset of lineage I Listeria monocytogenes

Genetic locus for streptolysin S production by group A streptococcus.

Thiazole and oxazole peptides: biosynthesis and molecular machinery.

Reduced virulence of group A streptococcal Tn916 mutants that do not produce streptolysin S

A global assembly line for cyanobactins

Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection.

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13004-13012

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10.1074/JBC.M900802200

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19

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284

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Morgan A. Pence

Douglas A Mitchell

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2009-03-13T00:00:00Z

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24201237

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19286651

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2676033

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