Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae.
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Role of Protein Phosphorylation in the Regulation of Cell Cycle and DNA-Related Processes in BacteriaSer/Thr phosphorylation as a regulatory mechanism in bacteriaAutophosphorylation of the Bacterial Tyrosine-Kinase CpsD Connects Capsule Synthesis with the Cell Cycle in Streptococcus pneumoniaeInterplay of the serine/threonine-kinase StkP and the paralogs DivIVA and GpsB in pneumococcal cell elongation and divisionProtein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talkRequirement of essential Pbp2x and GpsB for septal ring closure in Streptococcus pneumoniae D39.MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae.Gluconate 5-dehydrogenase (Ga5DH) participates in Streptococcus suis cell division.Mycoplasma pneumoniae, an underutilized model for bacterial cell biologyLocZ is a new cell division protein involved in proper septum placement in Streptococcus pneumoniae.Protein kinase A (PknA) of Mycobacterium tuberculosis is independently activated and is critical for growth in vitro and survival of the pathogen in the host.Remodeling of the Z-Ring Nanostructure during the Streptococcus pneumoniae Cell Cycle Revealed by Photoactivated Localization MicroscopyCharacterization of pneumococcal Ser/Thr protein phosphatase phpP mutant and identification of a novel PhpP substrate, putative RNA binding protein Jag.Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZThe Eukaryote-Like Serine/Threonine Kinase STK Regulates the Growth and Metabolism of Zoonotic Streptococcus suis.Streptococcus pneumoniae PBP2x mid-cell localization requires the C-terminal PASTA domains and is essential for cell shape maintenance.The physiology of bacterial cell division.Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation.From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?Nucleotide-independent cytoskeletal scaffolds in bacteria.How to get (a)round: mechanisms controlling growth and division of coccoid bacteria.Role of eukaryotic-like serine/threonine kinases in bacterial cell division and morphogenesis.Distribution of PASTA domains in penicillin-binding proteins and serine/threonine kinases of Actinobacteria.Exploring the diversity of protein modifications: special bacterial phosphorylation systems.Regulation of bacterial cell wall growth.Do Shoot the Messenger: PASTA Kinases as Virulence Determinants and Antibiotic Targets.Growth- and stress-induced PASTA kinase phosphorylation in Enterococcus faecalis.Phosphorylation of the cell division protein GpsB regulates PrkC kinase activity through a negative feedback loop in Bacillus subtilis.Interaction sites of DivIVA and RodA from Corynebacterium glutamicum.Pbp2x localizes separately from Pbp2b and other peptidoglycan synthesis proteins during later stages of cell division of Streptococcus pneumoniae D39Roles of the essential protein FtsA in cell growth and division in Streptococcus pneumoniae.Protein-protein interaction domains of Bacillus subtilis DivIVA.A programmed cell division delay preserves genome integrity during natural genetic transformation in Streptococcus pneumoniae.PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae.Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments.A visual review of the human pathogen Streptococcus pneumoniae.Interaction of Penicillin-Binding Protein 2x and Ser/Thr protein kinase StkP, two key players in Streptococcus pneumoniae R6 morphogenesis.Identification of EloR (Spr1851) as a regulator of cell elongation in Streptococcus pneumoniae.The GpsB files: the truth is out there.Suppression and synthetic-lethal genetic relationships of ΔgpsB mutations indicate that GpsB mediates protein phosphorylation and penicillin-binding protein interactions in Streptococcus pneumoniae D39.
P2860
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P2860
Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Mutational dissection of the S ...... n of Streptococcus pneumoniae.
@en
Mutational dissection of the S ...... n of Streptococcus pneumoniae.
@nl
type
label
Mutational dissection of the S ...... n of Streptococcus pneumoniae.
@en
Mutational dissection of the S ...... n of Streptococcus pneumoniae.
@nl
prefLabel
Mutational dissection of the S ...... n of Streptococcus pneumoniae.
@en
Mutational dissection of the S ...... n of Streptococcus pneumoniae.
@nl
P2093
P2860
P1476
Mutational dissection of the S ...... n of Streptococcus pneumoniae.
@en
P2093
Aurore Fleurie
Caroline Cluzel
Céline Freton
Frédéric Galisson
Isabelle Zanella-Cleon
Sébastien Guiral
P2860
P304
P356
10.1111/J.1365-2958.2011.07962.X
P407
P577
2012-01-11T00:00:00Z