Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
about
Sinorhizobium meliloti CpdR1 is critical for co-ordinating cell cycle progression and the symbiotic chronic infectionSegregation of molecules at cell division reveals native protein localization.McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpPMismatch repair causes the dynamic release of an essential DNA polymerase from the replication forkThe trpE gene negatively regulates differentiation of heterocysts at the level of induction in Anabaena sp. strain PCC 7120.Metabolic regulation via enzyme filamentationGenetic and cytological evidence that heterocyst patterning is regulated by inhibitor gradients that promote activator decay.Imaging mismatch repair and cellular responses to DNA damage in Bacillus subtilis.Regulated proteolysis in bacterial development.Hyperstructure interactions influence the virulence of the type 3 secretion system in yersiniae and other bacteria.Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis.A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum.Opposing effects of DNA on proteolysis of a replication initiator.Mutations in the Bacillus subtilis beta clamp that separate its roles in DNA replication from mismatch repair.ClpB1 overproduction in Synechocystis sp. strain PCC 6803 increases tolerance to rapid heat shock.ClpXP and ClpAP proteolytic activity on divisome substrates is differentially regulated following the Caulobacter asymmetric cell division.Polar localization and compartmentalization of ClpP proteases during growth and sporulation in Bacillus subtilis.Subcellular localization of RNA degrading proteins and protein complexes in prokaryotes.Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.
P2860
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P2860
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
description
2008 nî lūn-bûn
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2008年の論文
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2008年論文
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2008年論文
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2008年論文
@zh-hk
2008年論文
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2008年論文
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2008年论文
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2008年论文
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2008年论文
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name
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
@en
type
label
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
@en
prefLabel
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
@en
P2860
P356
P1476
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis
@en
P2093
Alan D Grossman
Lyle A Simmons
P2860
P304
P356
10.1128/JB.00590-08
P407
P50
P577
2008-08-08T00:00:00Z