Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
about
Activities and regulation of peptidoglycan synthasesThe Intimin periplasmic domain mediates dimerisation and binding to peptidoglycanPenicillin-binding proteins and bacterial resistance to beta-lactamsLocalization of PBP3 in Caulobacter crescentus is highly dynamic and largely relies on its functional transpeptidase domain.Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli.Elucidation of the structure of the membrane anchor of penicillin-binding protein 5 of Escherichia coliDaughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coliReactivation of peptidoglycan synthesis in ether-permeabilized Escherichia coli after inhibition by beta-lactam antibiotics.Peptidoglycan hydrolases of Escherichia coli.Peptidoglycan structure of Lactobacillus casei, a species highly resistant to glycopeptide antibiotics.Abnormal peptidoglycan produced in a methicillin-resistant strain of Staphylococcus aureus grown in the presence of methicillin: functional role for penicillin-binding protein 2A in cell wall synthesis.Changes in peptidoglycan composition and penicillin-binding proteins in slowly growing Escherichia coli.Forming cross-linked peptidoglycan from synthetic gram-negative Lipid IIEndopeptidase penicillin-binding proteins 4 and 7 play auxiliary roles in determining uniform morphology of Escherichia coliEscherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis.Peptidoglycan synthesis during the cell cycle of Escherichia coli: composition and mode of insertion.A simple gel electrophoretic method for analyzing the muropeptide composition of bacterial peptidoglycan.Penicillin-binding proteins of Haemophilus ducreyi.PBP1B Glycosyltransferase and Transpeptidase Activities Play Different Essential Roles during the De Novo Regeneration of Rod Morphology in Escherichia coli.In vitro synthesis of cross-linked murein and its attachment to sacculi by PBP1A from Escherichia coli.
P2860
Q26786994-EE817236-5F03-43FC-B6A1-A888E8DC5AAEQ27695738-A28A35FC-01A6-42C3-A5CD-39A1C321FFEBQ28257231-2E1F756C-CDC1-42D1-886C-7A2627DCE254Q30484481-4405C571-12E5-4C6D-8CAF-BD2E2A4B9E88Q30804047-DFCE855E-82A3-43BB-B0E0-202399C10B97Q33821568-046F969E-159D-49E8-9DB0-6BCEBEBC9075Q34976665-D2C7CB41-9B33-4F36-8CEB-6D290A0B843AQ35363665-6F300FD9-443B-422F-A028-2941A248CBC2Q35598330-6834BC0A-55F9-4C5A-9943-27415D2DDF23Q35631159-C692CC44-E7EA-41E4-A8E0-B91C90A51ABAQ35809167-2CB264A2-7350-4CB6-A183-CAF5B47DBF01Q36272551-8913863B-2175-4909-B6D4-1EBE7B50F9E6Q36857359-61B89451-7927-48E4-800F-A7ADF4935738Q37663628-0D30633D-AA87-4EB7-AE07-CF41D1F74475Q39496341-A3C0CDF7-DFBE-4A98-8E08-B578C3CB063CQ39950701-4A7457AF-657D-43AD-A54F-92E1867D47F4Q40024490-47366BDC-C7D0-4650-AB3A-A9DB65E4AEFCQ40284128-560D08B9-DA7D-4F32-8B27-5181E0C2B2D9Q41746382-6A41A02B-2B25-4EC4-918B-8F7917A1B204Q48086083-44C4D165-57E8-47C3-9C65-07C3DF12EE87
P2860
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年学术文章
@wuu
1987年学术文章
@zh-cn
1987年学术文章
@zh-hans
1987年学术文章
@zh-my
1987年学术文章
@zh-sg
1987年學術文章
@yue
1987年學術文章
@zh
1987年學術文章
@zh-hant
name
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
@en
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
@nl
type
label
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
@en
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
@nl
prefLabel
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
@en
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
@nl
P2860
P1476
Two distinct transpeptidation reactions during murein synthesis in Escherichia coli.
@en
P2093
P2860
P304
P356
10.1128/JB.169.7.3099-3103.1987
P577
1987-07-01T00:00:00Z