scholarly article | Q13442814 |
P2093 | author name string | Dalbey RE | |
R. E. Dalbey | |||
J. K. Laws | |||
Laws JK | |||
P2860 | cites work | Construction of Biologically Functional Bacterial Plasmids In Vitro | Q24562887 |
The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence | Q33573182 | ||
Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli | Q33655946 | ||
The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology | Q33880780 | ||
Topogenic signals in integral membrane proteins | Q34167358 | ||
Determinants of membrane protein topology | Q34372343 | ||
Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor | Q36245224 | ||
NH2-terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocation | Q36256980 | ||
Intracellular protein topogenesis | Q36360251 | ||
The Assembly of Proteins into Biological Membranes: The Membrane Trigger Hypothesis | Q38000320 | ||
Secretion and membrane localization of proteins in Escherichia coli. | Q40285614 | ||
Import of honeybee prepromelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein. | Q41345662 | ||
Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins | Q41564569 | ||
The transmembrane segment of the human transferrin receptor functions as a signal peptide. | Q42571061 | ||
Primary structure and transmembrane orientation of the murine anion exchange protein | Q43489711 | ||
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes | Q43822332 | ||
The internal signal sequence of Escherichia coli leader peptidase is necessary, but not sufficient, for its rapid membrane assembly | Q46238232 | ||
A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli | Q48342898 | ||
High-level expression of M13 gene II protein from an inducible polycistronic messenger RNA. | Q48382462 | ||
Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope | Q48395760 | ||
Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane. | Q52457501 | ||
Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly. | Q52493373 | ||
Multiple mechanisms of protein insertion into and across membranes. | Q53779152 | ||
Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane of Escherichia coli. | Q54764861 | ||
An artificial anchor domain: hydrophobicity suffices to stop transfer. | Q54796961 | ||
An internal signal sequence: The asialoglycoprotein receptor membrane anchor | Q56775313 | ||
Foreign transmembrane peptides replacing the internal signal sequence of transferrin receptor allow its translocation and membrane binding | Q57849730 | ||
The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domain | Q68891385 | ||
The role of the polar, carboxyl-terminal domain of Escherichia coli leader peptidase in its translocation across the plasma membrane | Q68901815 | ||
Many random sequences functionally replace the secretion signal sequence of yeast invertase | Q68925585 | ||
Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli | Q69881818 | ||
Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli. Relation to the orientation of membrane proteins | Q70229449 | ||
Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli | Q70257285 | ||
Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein | Q72125855 | ||
The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme | Q72932795 | ||
P433 | issue | 7 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
P304 | page(s) | 2095-2099 | |
P577 | publication date | 1989-07-01 | |
P1433 | published in | The EMBO Journal | Q1278554 |
P1476 | title | Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal | |
P478 | volume | 8 |
Q37613694 | A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli |
Q36685188 | Charge composition features of model single-span membrane proteins that determine selection of YidC and SecYEG translocase pathways in Escherichia coli |
Q35930775 | Decoding signals for membrane protein assembly using alkaline phosphatase fusions |
Q33921342 | Mapping of catalytically important domains in Escherichia coli leader peptidase |
Q50463977 | Molecular cloning of the Salmonella typhimurium lep gene in Escherichia coli |
Q57381637 | Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes |
Q36777551 | Proteolysis in protein import and export: Signal peptide processing in eu-and prokaryotes |
Q34043693 | Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length |
Q33334929 | Sequence and TnphoA analysis of a Mycoplasma hyorhinis protein with membrane export function |
Q27691857 | The Sec translocase |
Q29615298 | The complete general secretory pathway in gram-negative bacteria |
Q37942677 | The signal peptide |
Q40890215 | The topological analysis of integral cytoplasmic membrane proteins |
Q37694639 | The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism |
Q37636890 | Translocation of N-terminal tails across the plasma membrane |
Q44417229 | Translocation of Phospholipids Is Facilitated by a Subset of Membrane-spanning Proteins of the Bacterial Cytoplasmic Membrane |
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