An Escherichia coli mutant with an amino acid alteration within the signal sequence of outer membrane prolipoprotein.
about
A deletion that includes the segment coding for the signal peptidase cleavage site delays release of Saccharomyces cerevisiae acid phosphatase from the endoplasmic reticulumSurface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope.Mechanisms of protein localization.Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli.Prolipoprotein signal peptidase of Escherichia coli requires a cysteine residue at the cleavage site.Export without proteolytic processing of inner and outer membrane proteins encoded by F sex factor tra cistrons in Escherichia coli minicellsAssembly of outer membrane lipoprotein in an Escherichia coli mutant with a single amino acid replacement within the signal sequence of prolipoprotein.A mutation downstream from the signal peptidase cleavage site affects cleavage but not membrane insertion of phage coat proteinThe umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational couplingTemperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process.Chimeric influenza virus hemagglutinin containing either the NH2 terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surfacePost-translational modification and processing of Escherichia coli prolipoprotein in vitro.Alkaline phosphatase and OmpA protein can be translocated posttranslationally into membrane vesicles of Escherichia coli.Escherichia coli pleiotropic mutant that reduces amounts of several periplasmic and outer membrane proteinsGlobomycin sensitivity of Escherichia coli and Salmonella typhimurium: effects of mutations affecting structures of murein lipoprotein.Expression of a Streptococcus mutans glucosyltransferase gene in Escherichia coliInhibition of secretion of a mutant lipoprotein across the cytoplasmic membrane by the wild-type lipoprotein of the Escherichia coli outer membraneMechanism of protein excretion by gram-negative bacteria: Pseudomonas aeruginosa exotoxin A.Lipoprotein synthesis in Escherichia coli spheroplasts: accumulation of lipoprotein in cytoplasmic membrane.Inhibition of preprotein processing in ascites tumor lysates by incorporation of a leucine analog.Synthesis and maturation of lambda receptor in Escherichia coli K-12: in vivo and in vitro expression of gene lamB under lac promoter controlIntracellular protein topogenesis.DNA sequence encoding the NH2-terminal peptide involved in transport of lambda receptor, an Escherichia coli secretory proteinEukaryotic signal sequence transports insulin antigen in Escherichia coli.Bacteria mature preproinsulin to proinsulin.The four cytoplasmically made subunits of yeast mitochondrial cytochrome c oxidase are synthesized individually and not as a polyprotein.Export of protein in bacteria.Linkage map of Escherichia coli K-12, edition 6Membrane biogenesis: cotranslational integration of the bacteriophage f1 coat protein into an Escherichia coli membrane fraction.Neuroactive drugs inhibit trypsin and outer membrane protein processing in Escherichia coli K-12.ATP is essential for protein translocation into Escherichia coli membrane vesicles.Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein.Suppression of the lethal effect of acidic-phospholipid deficiency by defective formation of the major outer membrane lipoprotein in Escherichia coli.Nucleotide sequence of the gene encoding pilin of Bacteroides nodosus, the causal organism of ovine footrot.Processing mechanisms in the biosynthesis of proteins.A deletion that includes the signal peptidase cleavage site impairs processing, glycosylation, and secretion of cell surface yeast acid phosphatase.An inner membrane protein N-terminal signal sequence is able to promote efficient localisation of an outer membrane protein in Escherichia coli.The pro- and mature forms of the E. coli K-12 outer membrane phospholipase A are identical.Predicted secondary structures of amino-terminal extension sequences of secreted proteins.Post-translational processing of full-length presecretory proteins with canine pancreatic signal peptidase.
P2860
Q27939126-25F29473-A944-4DC7-9FE2-98AF06CDD7F8Q33538951-C65E98D2-C1C2-4B8B-8C71-08682377ED77Q33628061-BEEBFF23-8B8E-422D-9C53-89F87AB1A53FQ33655946-B885EAFA-5C7D-4D56-B749-3CC579460305Q33933295-5F97FAB9-7753-4907-891B-A349492D5118Q34034077-0BC277FE-3AAC-4277-B83F-C7B646D274A5Q34115380-4AA27831-AE22-4B64-96EC-DE8232F8B9BDQ35329853-CA065068-98D2-4995-BD77-1AA2D23C6CE2Q35582310-152FBE61-B033-497E-A7F3-7B8B297E969EQ36175678-2543DCF9-B088-44F9-AC2E-FA1A3042F115Q36247038-6A5A5C39-DF81-4612-B9BE-29840A3BEB86Q36289591-344DE306-9C6A-42A7-8E68-54AEB06FA904Q36291724-4D410FB1-C184-443D-86C9-494C3A9680D5Q36313239-536A7C36-40A5-4D61-A1E6-6ED12D84FE90Q36324014-7419E0D7-1FFE-4EEB-810D-2DEA073C9D6BQ36324665-16CC421C-BD4C-4E5D-A88A-BDFF7946E137Q36331424-F86E72B9-9651-45F6-A597-3E99D73A1561Q36332901-D9EE2441-4E72-4FFA-8F61-6570F87EE0E2Q36339295-49E448AC-4A9B-4B42-9DF1-05465FBAAF63Q36359487-538BBF55-2210-4E9D-B52C-C6374777C3DAQ36360232-C439F3B5-4651-4682-A72A-B623D01A8731Q36360251-EA9B30B0-E2CC-48A2-B650-8520A7BC614EQ36388227-1D0F33BF-0CC5-4EAB-925B-E1C98B101CACQ36393301-D283DB47-96E0-4EDB-A3C0-F9A7C96E222CQ36397167-A1C2048F-9FD5-40CC-B1BD-182725A316CCQ36398271-D85A7CFA-A6B6-4887-95DF-FF9A1749354DQ37066542-C2529BC1-1B58-4753-9584-6FC54BA0125CQ37066767-C9A952C2-B817-4EC6-BF2F-663119B8C5BDQ37320606-99CAD0E7-2650-4523-890B-60E5DD972602Q37329657-B66D671F-C5CC-4AE5-98F6-E03A7B775027Q37522633-2D763FA9-7B36-4867-9DD4-517C009BF69AQ37595620-276808DF-5B72-4555-BE04-0A16ACFCEF58Q39951286-0C8AC755-082C-451A-943B-03F0888540C7Q39969848-0BBD2C15-85C0-4871-8EF1-B379A65902BAQ40287053-8464B05A-7E6E-49BB-A983-85C7AACAD5B1Q40677029-EAF67A0A-5C3D-41A3-8BD7-9DC84D43F08DQ41416098-8C388886-7278-467C-B0F0-9D3063981BF1Q41577513-B8D9712C-1922-448D-91C7-0B5810FE000EQ41734750-1B9CCB81-ACE4-4E30-B3DA-6F04AC00B292Q49487608-A37E148E-B0A9-469B-A302-B8F7E6B5B848
P2860
An Escherichia coli mutant with an amino acid alteration within the signal sequence of outer membrane prolipoprotein.
description
1978 nî lūn-bûn
@nan
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
1978年论文
@zh
1978年论文
@zh-cn
name
An Escherichia coli mutant wit ...... outer membrane prolipoprotein.
@ast
An Escherichia coli mutant wit ...... outer membrane prolipoprotein.
@en
type
label
An Escherichia coli mutant wit ...... outer membrane prolipoprotein.
@ast
An Escherichia coli mutant wit ...... outer membrane prolipoprotein.
@en
prefLabel
An Escherichia coli mutant wit ...... outer membrane prolipoprotein.
@ast
An Escherichia coli mutant wit ...... outer membrane prolipoprotein.
@en
P2093
P2860
P356
P1476
An Escherichia coli mutant wit ...... outer membrane prolipoprotein.
@en
P2093
P2860
P304
P356
10.1073/PNAS.75.10.4891
P407
P577
1978-10-01T00:00:00Z