Difference between revisions of "PMID:6760806"
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| + | {| id="M4fdfc11dac09f" class=" tableEdit PMID_info_table" | ||
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| + | !align=left |Citation | ||
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| + | '''Jaffe, A, Chabbert, YA and Semonin, O''' (1982) Role of porin proteins OmpF and OmpC in the permeation of beta-lactams.''Antimicrob. Agents Chemother.'' '''22''':942-8 | ||
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| + | !align=left |Abstract | ||
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| + | Mutants of Escherichia coli K-12 lacking major outer membrane proteins were obtained by selecting for resistance to the beta-lactam cefoxitin. Three classes of resistant strains were found: mutants in ompB, a regulatory locus for proteins OmpF and OmpC; mutants in ompF; and one mutant in tpo. The OmpF and OmpC proteins facilitate penetration of beta-lactams through the outer membrane. | ||
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| + | !align=left |Links | ||
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| + | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6760806 PubMed] | ||
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| + | !align=left |Keywords | ||
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| + | Anti-Bacterial Agents; Bacterial Outer Membrane Proteins; Bacterial Proteins; Carrier Proteins; Cell Membrane Permeability; Escherichia coli; Hexosyltransferases; Membrane Proteins; Microbial Sensitivity Tests; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptidyl Transferases; beta-Lactams | ||
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| + | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.3214.M4fdfc11dac09f--> | ||
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| + | ==Main Points of the Paper == | ||
| + | {{LitSignificance}} | ||
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| + | == Materials and Methods Used == | ||
| + | {{LitMaterials}} | ||
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| + | ==Phenotype Annotations== | ||
| + | {{AnnotationTableHelp}} | ||
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| + | {| id="H4fdfc11daf04a" class=" tableEdit Phenotype_Table_2" | ||
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| + | !|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status | ||
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| + | ==Notes== | ||
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| + | ==References== | ||
| + | {{RefHelp}} | ||
| + | <references/> | ||
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| + | [[Category:Publication]] | ||
Revision as of 19:00, 18 June 2012
| Citation |
Jaffe, A, Chabbert, YA and Semonin, O (1982) Role of porin proteins OmpF and OmpC in the permeation of beta-lactams.Antimicrob. Agents Chemother. 22:942-8 |
|---|---|
| Abstract |
Mutants of Escherichia coli K-12 lacking major outer membrane proteins were obtained by selecting for resistance to the beta-lactam cefoxitin. Three classes of resistant strains were found: mutants in ompB, a regulatory locus for proteins OmpF and OmpC; mutants in ompF; and one mutant in tpo. The OmpF and OmpC proteins facilitate penetration of beta-lactams through the outer membrane. |
| Links | |
| Keywords |
Anti-Bacterial Agents; Bacterial Outer Membrane Proteins; Bacterial Proteins; Carrier Proteins; Cell Membrane Permeability; Escherichia coli; Hexosyltransferases; Membrane Proteins; Microbial Sensitivity Tests; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptidyl Transferases; beta-Lactams |
| edit table |
Main Points of the Paper
Please summarize the main points of the paper.
Materials and Methods Used
Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).
Phenotype Annotations
See Help:AnnotationTable for details on how to edit this table.
<protect>
| Phenotype of | Taxon Information | Genotype Information (if known) | Condition Information | OMP ID | OMP Term Name | ECO ID | ECO Term Name | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|
| edit table |
</protect>
Notes
References
See Help:References for how to manage references in omp dev.
