FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. - Wikidata - awgldk - TriplyDB

FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit.

FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit.

http://www.wikidata.org/entity/Q34342148

about

Phage lambda CIII: a protease inhibitor regulating the lysis-lysogeny decision Recent findings about the Yersinia enterocolitica phage shock protein response Structure, Binding, and Activity of Syd, a SecY-interacting Protein Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Arabidopsis florigen FT binds to diurnally oscillating phospholipids that accelerate flowering.Recombination-based in vivo expression technology identifies Helicobacter pylori genes important for host colonization FtsH--a single-chain charonin?Co-evolution of multipartite interactions between an extended tmRNA tag and a robust Lon protease in Mycoplasma.Characterization of the cvaA and cvi promoters of the colicin V export system: iron-dependent transcription of cvaA is modulated by downstream sequences Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay.Streptococcus pyogenes polymyxin B-resistant mutants display enhanced ExPortal integrity.Role of the sporulation protein BofA in regulating activation of the Bacillus subtilis developmental transcription factor sigmaK Escherichia coli translocase: the unravelling of a molecular machine.Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell.Proton-motive force stimulates the proteolytic activity of FtsH, a membrane-bound ATP-dependent protease in Escherichia coli Functional expression of miraculin, a taste-modifying protein in Escherichia coli.Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY.Mechanisms of integral membrane protein insertion and folding Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coli The bacterial Sec-translocase: structure and mechanism.An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY Membrane proteases in the bacterial protein secretion and quality control pathway.Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA).Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Links between type III secretion and extracytoplasmic stress responses in Yersinia Dual role of the metalloprotease FtsH in biogenesis of the DrrAB drug transporter.ATP-dependent proteases differ substantially in their ability to unfold globular proteins Quality control of cytoplasmic membrane proteins in Escherichia coli.RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences.HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae.FtsH proteases located in the plant chloroplast.Breaking on through to the other side: protein export through the bacterial Sec system.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli.Evidence for an active role of the DnaK chaperone system in the degradation of sigma(32).Comparative proteomic analysis of high cell density cultivations with two recombinant Bacillus megaterium strains for the production of a heterologous dextransucrase.Protein secretion in Corynebacterium glutamicum.

P2860

Q21144758-FD38CAC4-D18D-4A84-8D50-A0CB58FB7663 Q27025626-BEB1139B-EB80-466E-8687-7E91259C0974 Q27653403-4DDBE036-947B-4771-AF11-405D8011A34D Q27939649-E1481238-7F3F-4B63-B983-CF87ECEF9D5F Q28488804-3E6E2570-6ECE-405C-8912-D81018EB9280 Q30153518-210957C0-A67E-4BB2-95FA-FFD5480CCC08 Q33358179-4E9C89A7-1166-40BC-A565-00A8C031C102 Q33369702-F87BCF56-D9D7-4917-8BCF-C5808997E56E Q33541350-F0D10774-191B-44FA-B4CC-289C31451BE0 Q33591989-C68D340D-A401-4C85-BFDF-501021B37A13 Q33727255-A7E924F3-4C20-423C-903A-EFFE0081FF60 Q33728173-3332CFC6-AA57-475C-9289-069416A58B73 Q33899541-63974A5F-19CB-4477-9E8E-E393AFDDF833 Q33992850-0ACEF4E4-2ABD-46C4-B005-528BF4927C4D Q33994549-94DFCFF2-E0CD-4819-8137-B24F08339D37 Q33996303-EFD10B6D-4085-4748-980F-490152245BEF Q34031176-BDF672BB-884E-4903-908E-4E89C3DE2A76 Q34915004-3D267128-FF6D-4057-A359-C300352805B4 Q34996061-D826824D-9BEE-4201-85D0-1C393B9C1D05 Q35118815-EF81715E-8D0E-476A-B6DB-58F965BBEEA4 Q35198523-37002707-CDF5-4F5B-9F99-5668EF8CFD76 Q35598781-7774B553-CFE2-40EB-8ED6-FF682F2F2001 Q35814696-3219D33A-9314-486E-942C-7516C7F23771 Q35865651-AF110D38-51CB-4F4D-8E67-6191CAAF76AA Q36023269-FBEBEC7C-705A-4A6D-9E15-7F90DB4CB71F Q36150293-A75CCC44-4538-46C3-B15D-51A6596DC6B2 Q36155063-2F5C447F-82B8-42B9-9A82-B574737A55A8 Q36306773-DE303C18-B160-4F8D-BFF0-5690584C5CE1 Q36796824-533593EA-309A-4AB9-8F2B-5BF59AFE9E29 Q37254059-48A40099-2F4B-41FC-8971-863F43D93EA2 Q37489256-F7F5A478-D36D-400F-AEAE-32BE7D7EB29B Q37605202-8250A80E-5165-45FC-9DC6-0887CB4B5698 Q37663408-A04ACE0F-627A-4788-A496-20C25F99A82A Q37961719-279E778E-B84C-467E-9EBB-727EA32B33AD Q38065265-5FA07D44-45F1-42A7-B756-6E9F102A2177 Q38206834-487A5151-04B2-49E1-A86D-1ED12D7DE0BB Q38290596-4D141334-5C22-4765-AAFC-D20CAFCD5497 Q38496040-0BA66CAD-7C5F-431E-B1EA-69D147856717 Q38841551-482C7D6F-95EA-418A-9491-ECA934E71F91 Q38979795-B6DCC4FC-60AD-4B9A-9907-E9FD95327636

P2860

FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit.

http://www.wikidata.org/entity/Q34342148

description

1995 nî lūn-bûn

@nan

1995 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի մայիսին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

name

FtsH is required for proteolyt ...... l protein translocase subunit.

@ast

FtsH is required for proteolyt ...... l protein translocase subunit.

@en

FtsH is required for proteolyt ...... l protein translocase subunit.

@nl

type

label

FtsH is required for proteolyt ...... l protein translocase subunit.

@ast

FtsH is required for proteolyt ...... l protein translocase subunit.

@en

FtsH is required for proteolyt ...... l protein translocase subunit.

@nl

prefLabel

FtsH is required for proteolyt ...... l protein translocase subunit.

@ast

FtsH is required for proteolyt ...... l protein translocase subunit.

@en

FtsH is required for proteolyt ...... l protein translocase subunit.

@nl

P1433

Q34342148-9E1C0AD4-0ECA-42DD-AD5F-3F71978BA7C5

P1476

Q34342148-9F1FDAEA-A4F1-4490-AFB9-307F13B44364

P2093

Q34342148-639FF66B-76D3-479C-8655-66DD7EFF431D

Q34342148-D52C5B45-C28C-448F-A551-2467DB009219

P2860

Q34342148-049C9553-88F5-4A44-95A8-0B2D493AF1BE

Q34342148-0B389404-4C7D-4950-B17F-AE73FD45D6CF

Q34342148-0C8B0560-EF66-4C8D-8D51-E9B9BD643437

Q34342148-143C96E1-BE2D-49CF-8FCA-CAC889DD72C4

Q34342148-17FD3F05-5DC8-4048-8125-6FFB76B0BE22

Q34342148-20AD1FB1-CB8D-42BA-BCDF-B65185B58371

Q34342148-216AEDDF-2F5D-4242-91C5-62CD3B6EE0E9

Q34342148-26886BB7-C55F-435A-994C-D06BED05A319

Q34342148-3033F378-E2E7-4D14-97ED-80CAEBDED330

Q34342148-38838159-420E-4F5B-BF76-2532D211A0EF

P304

Q34342148-B393FD70-615D-46D7-A466-23901041C305

P31

Q34342148-1929A71D-0141-4C35-8C4A-23A870F83E15

P356

Q34342148-5FE5F65F-0E94-481F-8E19-FE0BD8DABDF0

P407

Q34342148-5400EDBA-9DED-45A3-B4D3-4D9B312332FC

P433

Q34342148-79D30F7C-A7DA-4873-978A-AA0B54A2AC30

P478

Q34342148-2246CD8B-8822-4CF5-A12C-DEF5A0B2C0E9

P50

Q34342148-4E3543E8-A382-488D-8393-C525BED8158C

P577

Q34342148-D5FF56A2-D70A-4C80-AE38-F8D7A86D5BD8

P5875

Q34342148-8E73BC02-58A1-4321-B72F-F8F53C077218

P698

Q34342148-77B2A292-021F-426E-9EB3-6F8C13D61B0C

P921

Q34342148-E5DE4E1F-C42A-4D80-8900-85F2C5A7B36C

P932

Q34342148-092DB241-0059-4AA2-BDC4-662FCD6535FF

P356

PNAS.92.10.4532

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

FtsH is required for proteolyt ...... l protein translocase subunit.

@en

P2093

K Ito

http://www.w3.org/2001/XMLSchema#string

Y Akiyama

http://www.w3.org/2001/XMLSchema#string

P2860

Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase family

Isolation of a differentially regulated splicing isoform of human NF-E2

BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae

Intramitochondrial protein sorting. Isolation and characterization of the yeast MSP1 gene which belongs to a novel family of putative ATPases.

A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum.

S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase

Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.

A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant.

Properties of the translocatable tetracycline-resistance element Tn10 in Escherichia coli and bacteriophage lambda.

PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains

P304

4532-4536

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.92.10.4532

http://www.w3.org/2001/XMLSchema#string

P407

P433

10

http://www.w3.org/2001/XMLSchema#string

P478

92

http://www.w3.org/2001/XMLSchema#string

P50

P577

1995-05-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

15445030

http://www.w3.org/2001/XMLSchema#string

P698

7753838

http://www.w3.org/2001/XMLSchema#string

P921

P932

41978

http://www.w3.org/2001/XMLSchema#string