Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli.
about
Evolution of penicillin-binding protein 2 concentration and cell shape during a long-term experiment with Escherichia coliFunctional taxonomy of bacterial hyperstructuresThe bacterial actin-like cytoskeletonThe PECACE domain: a new family of enzymes with potential peptidoglycan cleavage activity in Gram-positive bacteriaBacterial alpha2-macroglobulins: colonization factors acquired by horizontal gene transfer from the metazoan genome?Molecular mechanisms for the evolution of bacterial morphologies and growth modesCoarse-grained simulations of bacterial cell wall growth reveal that local coordination alone can be sufficient to maintain rod shape.Structure of a bacterial α2-macroglobulin reveals mimicry of eukaryotic innate immunityFormation of the glycan chains in the synthesis of bacterial peptidoglycanThe cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentusBacterial cell curvature through mechanical control of cell growth.Structure of protease-cleaved Escherichia coli α-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.Signature-tagged mutagenesis of Pasteurella multocida identifies mutants displaying differential virulence characteristics in mice and chickens.alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli.Adaptive mutations and replacements of virulence traits in the Escherichia coli O104:H4 outbreak population.Interaction and modulation of two antagonistic cell wall enzymes of mycobacteria.Analysis of glycan polymers produced by peptidoglycan glycosyltransferases.Beta-lactam antibiotics: from antibiosis to resistance and bacteriologyContributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli.Conformational states of a bacterial α2-macroglobulin resemble those of human complement C3.The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.Penicillin-binding proteins 1a and 1b form independent dimers in Escherichia coli.Bacterial cell wall synthesis: new insights from localization studiesAntimicrobial growth promoters used in animal feed: effects of less well known antibiotics on gram-positive bacteria.Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibioticsMonofunctional transglycosylases are not essential for Staphylococcus aureus cell wall synthesis.MtgA Deletion-Triggered Cell Enlargement of Escherichia coli for Enhanced Intracellular Polyester Accumulation.Skin and bones: the bacterial cytoskeleton, cell wall, and cell morphogenesisZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division.The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN.Function and localization dynamics of bifunctional penicillin-binding proteins in Caulobacter crescentus.A simple screen for murein transglycosylase inhibitors.The glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae catalyzes the polymerization of murein glycan chains.Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coliPBP1 is a component of the Bacillus subtilis cell division machinery.Diverse functions for six glycosyltransferases in Caulobacter crescentus cell wall assemblyKinetic characterization of the monofunctional glycosyltransferase from Staphylococcus aureus.Neisseria gonorrhoeae penicillin-binding protein 3 demonstrates a pronounced preference for N(epsilon)-acylated substrates.Development of an LC-MALDI method for the analysis of protein complexes.
P2860
Q24644443-850FD755-3103-4DDA-9F98-200DD8E220C1Q24671609-D3B6D87C-DFAD-4D57-8827-084A03D2E44BQ24672588-5A7209B1-E4B7-4031-B6DB-A968E48C113DQ24795323-97EDAA0F-9AF1-4149-BB9A-BA7A9EC3AA6DQ24804769-24ADF663-A67D-4E62-B0A9-5417C2C989B4Q27015816-748EC5BB-3262-4EFD-AA0E-B79B342D2287Q27323934-E3F1EEC6-9BD0-4C5C-9129-B59755FE01F8Q27695619-07A7C249-3B2E-42CC-8947-FD7997F88564Q28185380-DDC090E3-48DF-405D-9D90-F775DB188838Q29138524-EFDED04E-E32A-49AE-84F4-0F6E7C4EE525Q30487655-B314D1B8-F2DB-4783-9D8A-39B8B59CD7A9Q30657443-E0961D83-52CD-4FDC-8495-553C84181169Q30786556-A69B8B49-4AD2-44F8-A41E-93DCCB174AB8Q33359475-56D4A63E-E084-415E-9A14-EB47B1ECC7D4Q33407752-C527C98D-5F7A-41BF-A3E8-42ADD845177BQ33649862-F9DAE3E5-97EC-47A8-AFE3-E43C11CEDB6DQ33724376-5CF49D72-F361-4019-8540-FF43E3C948BEQ33951933-D3D4F258-DCCD-4B4E-BBA4-4D8598E490A9Q33996163-390F1951-3396-4B8E-9817-865A918F432FQ34243701-D97EDC30-0B58-4CDC-9185-965C1641F3FCQ34297837-C9B49410-E821-405C-8B0F-9C7FA0A393F0Q34300761-A5AB2C56-9F14-455B-814B-E273DAE190E9Q34313500-2BF33968-1DA4-4705-9235-AC7C172F227AQ34474627-15915F53-595C-486D-8EE7-4C87A720718BQ34927077-E9658607-6C3B-4E75-95C3-09D9CF2F0AADQ34984274-80BB3D2D-6DA3-4727-AE67-3FD24783E000Q35096164-E632885E-0166-4652-8168-C180BBDDB81CQ35650973-A0C06DD5-C592-4F1A-9B4A-26CC507F2B83Q36119626-90AFE8C0-4D5D-4575-A0B7-BE8F02319ED8Q36276314-3994FD62-99DB-40ED-82A1-CE67CB213643Q36483203-AEF85E85-3D1A-41E6-912E-CBB6AA9C1994Q37713194-9F68F141-26F0-4301-830D-BDDAF2125EEFQ39473696-7E5AB198-59C4-419F-8058-93D3589F24C9Q39791499-A7C1C2BF-E8FD-4D44-B094-7D496A8125E1Q39887020-B5A85912-7A57-4974-AA6B-87EFB0CED54DQ41073510-90D82015-CEEE-4889-A09D-9BF1062D9AB4Q41830871-5A392127-DD3C-43C3-823A-547E8B1BB71BQ41855641-AF3F281F-4F70-49A4-A58B-EDD505DD8555Q41917672-3AA6054E-D1F7-435E-949D-8627549D559CQ44897206-738F1235-8839-4AA7-8E9C-32B0D9F35C77
P2860
Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Cloning and characterization o ...... proteins of Escherichia coli.
@ast
Cloning and characterization o ...... proteins of Escherichia coli.
@en
type
label
Cloning and characterization o ...... proteins of Escherichia coli.
@ast
Cloning and characterization o ...... proteins of Escherichia coli.
@en
prefLabel
Cloning and characterization o ...... proteins of Escherichia coli.
@ast
Cloning and characterization o ...... proteins of Escherichia coli.
@en
P2860
P356
P1476
Cloning and characterization o ...... proteins of Escherichia coli.
@en
P2093
P2860
P304
32031-32039
P356
10.1074/JBC.274.45.32031
P407
P577
1999-11-01T00:00:00Z