A free terminal carboxylate group is required for PhrA pentapeptide inhibition of RapA phosphatase (Q43757204)

26 November 2017

title

A free terminal carboxylate group is required for PhrA pentapeptide inhibition of RapA phosphatase (English)

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26 November 2017

2

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26 November 2017

Core LJ

1

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26 November 2017

Perego M

series ordinal

3

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26 November 2017

publication date

1 October 2001

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26 November 2017

number of pages

5

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inferred from page(s)

published in

Peptides

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26 November 2017

volume

22

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26 November 2017

issue

10

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26 November 2017

page(s)

1549-1553

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Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay

26 November 2017

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Cell-associated pheromone peptide (cCF10) production and pheromone inhibition in Enterococcus faecalis

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The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions

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Single-amino acid substitutions alter the specificity and affinity of PDZ domains for their ligands.

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Properties of a pentapeptide inhibitor of peptidyltransferase that is essential for cat gene regulation by translation attenuation

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Initiation of bacterial development

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Differential processing of propeptide inhibitors of Rap phosphatases in Bacillus subtilis

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Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis

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Crystal structure of the zeta isoform of the 14-3-3 protein

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The ermC leader peptide: amino acid alterations leading to differential efficiency of induction by macrolide-lincosamide-streptogramin B antibiotics

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Transcriptional regulation of Bacillus subtilis glucose starvation-inducible genes: control of gsiA by the ComP-ComA signal transduction system

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A peptide export-import control circuit modulating bacterial development regulates protein phosphatases of the phosphorelay

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Pentapeptide regulation of aspartyl-phosphate phosphatases

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Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis

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The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence

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Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis

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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

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Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

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Heterocyst pattern formation controlled by a diffusible peptide

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Identifiers

DOI

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26 November 2017

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