Literature DB >> 3280555

A progenitor of the outer membrane LamB trimer.

J Stader1, T J Silhavy.   

Abstract

During its localization to the outer membrane, LamB possesses distinctive biochemical properties as it passes through the cytoplasmic membrane. Because LamB entered this dynamic state with an attached signal sequence and leaves after cleavage, we call this export-related form of LamB the early-translocation form (et-LamB).

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Year:  1988        PMID： 3280555      PMCID： PMC211062          DOI： 10.1128/jb.170.4.1973-1974.1988

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


  14 in total

1.  Selective solubilization of proteins from red blood cell membranes by protein perturbants.

Authors:  T L Steck; J Yu
Journal:  J Supramol Struct       Date:  1973

2.  Evidence for specificity at an early step in protein export in Escherichia coli.

Authors:  C A Kumamoto; J Beckwith
Journal:  J Bacteriol       Date:  1985-07       Impact factor: 3.490

3.  Post-translational export of maltose-binding protein in Escherichia coli strains harboring malE signal sequence mutations and either prl+ or prl suppressor alleles.

Authors:  J P Ryan; P J Bassford
Journal:  J Biol Chem       Date:  1985-11-25       Impact factor: 5.157

4.  Assembly pathway of newly synthesized LamB protein an outer membrane protein of Escherichia coli K-12.

Authors:  G H Vos-Scheperkeuter; B Witholt
Journal:  J Mol Biol       Date:  1984-06-05       Impact factor: 5.469

5.  Protein localization in E. coli: is there a common step in the secretion of periplasmic and outer-membrane proteins?

Authors:  K Ito; P J Bassford; J Beckwith
Journal:  Cell       Date:  1981-06       Impact factor: 41.582

6.  Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor.

Authors:  S D Emr; T J Silhavy
Journal:  J Mol Biol       Date:  1980-07-25       Impact factor: 5.469

7.  Purification and characterization of leader (signal) peptidase from Escherichia coli.

Authors:  C Zwizinski; W Wickner
Journal:  J Biol Chem       Date:  1980-08-25       Impact factor: 5.157

8.  Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: inhibition by higher oligosaccharides of maltose series.

Authors:  M Luckey; H Nikaido
Journal:  Biochem Biophys Res Commun       Date:  1980-03-13       Impact factor: 3.575

9.  E. coli mutant pleiotropically defective in the export of secreted proteins.

Authors:  D B Oliver; J Beckwith
Journal:  Cell       Date:  1981-09       Impact factor: 41.582

10.  Isolation of the bacteriophage lambda receptor from Escherichia coli.

Authors:  L Randall-Hazelbauer; M Schwartz
Journal:  J Bacteriol       Date:  1973-12       Impact factor: 3.490
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  11 in total

1.  Demonstration of a folded monomeric form of porin PhoE of Escherichia coli in vivo.

Authors:  P Van Gelder; J Tommassen
Journal:  J Bacteriol       Date:  1996-09       Impact factor: 3.490

2.  Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA.

Authors:  J L Huie; T J Silhavy
Journal:  J Bacteriol       Date:  1995-06       Impact factor: 3.490

Review 3.  The complete general secretory pathway in gram-negative bacteria.

Authors:  A P Pugsley
Journal:  Microbiol Rev       Date:  1993-03

4.  Identification, isolation, and characterization of the 42-kilodalton major outer membrane protein (MompA) from Treponema pectinovorum ATCC 33768.

Authors:  S G Walker; J L Ebersole; S C Holt
Journal:  J Bacteriol       Date:  1997-10       Impact factor: 3.490

5.  Analysis of the structure and subcellular location of filamentous phage pIV.

Authors:  M Russel; B Kaźmierczak
Journal:  J Bacteriol       Date:  1993-07       Impact factor: 3.490

6.  A new suppressor of a lamB signal sequence mutation, prlZ1, maps to 69 minutes on the Escherichia coli chromosome.

Authors:  S Q Wei; J Stader
Journal:  J Bacteriol       Date:  1994-09       Impact factor: 3.490

7.  The rare outer membrane protein, OmpL1, of pathogenic Leptospira species is a heat-modifiable porin.

Authors:  E S Shang; M M Exner; T A Summers; C Martinich; C I Champion; R E Hancock; D A Haake
Journal:  Infect Immun       Date:  1995-08       Impact factor: 3.441

8.  Suppressor analysis suggests a multistep, cyclic mechanism for protein secretion in Escherichia coli.

Authors:  K Bieker-Brady; T J Silhavy
Journal:  EMBO J       Date:  1992-09       Impact factor: 11.598

9.  The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis.

Authors:  J M Bolla; C Lazdunski; J M Pagès
Journal:  EMBO J       Date:  1988-11       Impact factor: 11.598

10.  LipL32 Is a Subsurface Lipoprotein of Leptospira interrogans: presentation of new data and reevaluation of previous studies.

Authors:  Marija Pinne; David A Haake
Journal:  PLoS One       Date:  2013-01-08       Impact factor: 3.240
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