scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.273.34.21675 |
P8608 | Fatcat ID | release_7plpb3lsbvga3njjykiaatcqse |
P698 | PubMed publication ID | 9705302 |
P50 | author | Jerry Eichler | Q56480904 |
P2093 | author name string | W Wickner | |
K Rinard | |||
P2860 | cites work | Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro | Q33678296 |
Site-specific antibodies against the PrlA (secY) protein of Escherichia coli inhibit protein export by interfering with plasma membrane binding of preproteins | Q33843679 | ||
Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery | Q33858303 | ||
Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme | Q33886664 | ||
The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling | Q33887254 | ||
Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli | Q34317954 | ||
The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface | Q36064136 | ||
SecYEG and SecA are the stoichiometric components of preprotein translocase | Q38292412 | ||
A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. | Q38336960 | ||
The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events | Q38339927 | ||
Biogenesis of the gram-negative bacterial envelope | Q41657961 | ||
SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane | Q41850974 | ||
SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study | Q41897858 | ||
The protease-protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase | Q41944218 | ||
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes | Q43822332 | ||
ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle | Q44556405 | ||
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. | Q46008320 | ||
The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane | Q46059428 | ||
ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase | Q46481993 | ||
Assembly of translocation-competent proteoliposomes from detergent-solubilized rough microsomes. | Q49486728 | ||
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. | Q52513940 | ||
Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. | Q54154827 | ||
Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding. | Q54559159 | ||
Identification of a region of interaction between Escherichia coli SecA and SecY proteins. | Q54567468 | ||
A significant fraction of functional SecA is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation. | Q54576716 | ||
SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm. | Q54577867 | ||
SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. | Q54598039 | ||
SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. | Q54627502 | ||
Separable ATPase and Membrane Insertion Domains of the SecA Subunit of Preprotein Translocase | Q57976575 | ||
P433 | issue | 34 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 21675-21681 | |
P577 | publication date | 1998-08-01 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Endogenous SecA catalyzes preprotein translocation at SecYEG | |
P478 | volume | 273 |
Q63359166 | A High-Resolution Luminescent Assay for Rapid and Continuous Monitoring of Protein Translocation across Biological Membranes |
Q33741843 | Amphitropic proteins: regulation by reversible membrane interactions (review). |
Q45947385 | An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets. |
Q42558513 | Competitive binding of the SecA ATPase and ribosomes to the SecYEG translocon. |
Q36652863 | Design, Synthesis and Evaluation of Triazole-Pyrimidine Analogues as SecA Inhibitors. |
Q35107369 | Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking |
Q33836404 | Dimeric SecA is essential for protein translocation |
Q73843659 | Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase |
Q43690465 | Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation |
Q54450403 | In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA. |
Q73626344 | Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations |
Q28535409 | Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channels |
Q34293903 | Protein translocation across membranes |
Q33893908 | Role of lipids in the translocation of proteins across membranes |
Q36793326 | Roles of SecG in ATP- and SecA-dependent protein translocation. |
Q63359819 | Sec Protein-Conducting Channel and SecA |
Q50307534 | SecA functions in vivo as a discrete anti-parallel dimer to promote protein transport. |
Q33807313 | SecA: the ubiquitous component of preprotein translocase in prokaryotes. |
Q33848928 | SecM facilitates translocase function of SecA by localizing its biosynthesis |
Q54480226 | Selective SecA association with signal sequences in ribosome-bound nascent chains: a potential role for SecA in ribosome targeting to the bacterial membrane. |
Q44155922 | Superactive SecY variants that fulfill the essential translocation function with a reduced cellular quantity. |
Q47684820 | The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions |
Q39568449 | The SecA subunit of Escherichia coli preprotein translocase is exposed to the periplasm |
Q42152267 | The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release |
Q54436102 | Topology inversion of SecG is essential for cytosolic SecA-dependent stimulation of protein translocation. |
Q44542398 | Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction |
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