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Literature DB >> 11344132

Polarity in action: asymmetric protein localization in bacteria.

S R Lybarger¹, J R Maddock.

Abstract

Mesh：

Substances：
Actins
Bacterial Proteins

Year: 2001 PMID： 11344132 PMCID： PMC99622 DOI： 10.1128/JB.183.11.3261-3267.2001

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

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102 in total

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4. Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus.

Authors: M R Alley; S L Gomes; W Alexander; L Shapiro
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5. Mucopeptide biosynthesis by minicells of Escherichia coli.

Authors: J N Reeve
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6. Effect of O side-chain length and composition on the virulence of Shigella flexneri 2a.

Authors: R C Sandlin; M B Goldberg; A T Maurelli
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7. Polar location of the chemoreceptor complex in the Escherichia coli cell.

Authors: J R Maddock; L Shapiro
Journal: Science Date: 1993-03-19 Impact factor: 47.728

8. Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin.

Authors: M L Bernardini; J Mounier; H d'Hauteville; M Coquis-Rondon; P J Sansonetti
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9. Alterations of murein structure and of penicillin-binding proteins in minicells from Escherichia coli.

Authors: W Obermann; J V Höltje
Journal: Microbiology Date: 1994-01 Impact factor: 2.777

10. Avirulence of rough mutants of Shigella flexneri: requirement of O antigen for correct unipolar localization of IcsA in the bacterial outer membrane.

Authors: R C Sandlin; K A Lampel; S P Keasler; M B Goldberg; A L Stolzer; A T Maurelli
Journal: Infect Immun Date: 1995-01 Impact factor: 3.441

48 in total

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2. Cooperativity between bacterial chemotaxis receptors.

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3. Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model.

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4. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity.

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5. Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.

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