scholarly article | Q13442814 |
P2093 | author name string | Miriam Braunstein | |
Henry S Gibbons | |||
Lauren S Ligon | |||
Meghan E Feltcher | |||
P2860 | cites work | Overlapping functions of components of a bacterial Sec-independent protein export pathway | Q24533263 |
SecA, a remarkable nanomachine | Q24631210 | ||
Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR | Q27649095 | ||
A common export pathway for proteins binding complex redox cofactors? | Q27976517 | ||
Signal peptidases | Q28217085 | ||
Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli | Q28299991 | ||
SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis | Q28487244 | ||
ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophages | Q28487421 | ||
Mycobacterium tuberculosis Rv2224c modulates innate immune responses | Q28487461 | ||
SignalP 4.0: discriminating signal peptides from transmembrane regions | Q29547202 | ||
Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis | Q29615255 | ||
SecA-dependent quality control of intracellular protein localization | Q31022756 | ||
Investigating the role of secA2 in secretion and glycosylation of a fimbrial adhesin in Streptococcus parasanguis FW213. | Q31095089 | ||
Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway | Q33232877 | ||
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli | Q33562047 | ||
Signal peptides are allosteric activators of the protein translocase | Q33662560 | ||
Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro | Q33678296 | ||
Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer | Q33773458 | ||
Competition between Sec- and TAT-dependent protein translocation in Escherichia coli | Q33890978 | ||
Translocation can drive the unfolding of a preprotein domain. | Q34041521 | ||
Transport of preproteins by the accessory Sec system requires a specific domain adjacent to the signal peptide | Q34045689 | ||
Modeling the effects of prl mutations on the Escherichia coli SecY complex | Q34048338 | ||
The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases | Q34124354 | ||
SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis | Q35003009 | ||
Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway | Q35022917 | ||
The antigen 85 complex: a major secretion product of Mycobacterium tuberculosis | Q35655414 | ||
Selective photoaffinity labeling identifies the signal peptide binding domain on SecA | Q35750297 | ||
The bacterial Sec-translocase: structure and mechanism. | Q35814696 | ||
Glycine residues in the hydrophobic core of the GspB signal sequence route export toward the accessory Sec pathway | Q35879231 | ||
A little help from my friends: quality control of presecretory proteins in bacteria | Q35933897 | ||
A genomic view of sugar transport in Mycobacterium smegmatis and Mycobacterium tuberculosis | Q35949975 | ||
A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec system | Q36097994 | ||
Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysis of a mycobacterial lgt mutant. | Q36156186 | ||
Emerging themes in SecA2-mediated protein export | Q36206572 | ||
Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm | Q36313695 | ||
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli | Q36326983 | ||
SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis | Q36350571 | ||
Evidence for specificity at an early step in protein export in Escherichia coli | Q36361933 | ||
The bacterial twin-arginine translocation pathway | Q36498300 | ||
Prediction of lipoprotein signal peptides in Gram-negative bacteria | Q36572165 | ||
Characterization of the accessory Sec system of Staphylococcus aureus | Q36898397 | ||
Beta-lactamase can function as a reporter of bacterial protein export during Mycobacterium tuberculosis infection of host cells | Q37082058 | ||
Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence | Q37232681 | ||
Mapping polypeptide interactions of the SecA ATPase during translocation | Q37428012 | ||
SecA: a tale of two protomers | Q37742750 | ||
The signal peptide | Q37942677 | ||
The twin-arginine translocation (Tat) protein export pathway | Q38017546 | ||
Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli | Q38290685 | ||
The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events | Q38339927 | ||
The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein | Q38347439 | ||
Two nonredundant SecA homologues function in mycobacteria. | Q39505468 | ||
Genetic Analysis of Pathway Specificity during Posttranslational Protein Translocation across the Escherichia coli Plasma Membrane | Q39750256 | ||
Identification of a regulated alkaline phosphatase, a cell surface-associated lipoprotein, in Mycobacterium smegmatis. | Q39793904 | ||
SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein | Q40388434 | ||
The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids | Q40871781 | ||
Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway | Q42412477 | ||
Identification of the preprotein binding domain of SecA. | Q42485674 | ||
The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal | Q42621979 | ||
Differential roles of individual domains in selection of secretion route of a Streptococcus parasanguinis serine-rich adhesin, Fap1. | Q42910236 | ||
The Accessory SecA2 System of Mycobacteria Requires ATP Binding and the Canonical SecA1. | Q43150590 | ||
A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif | Q43858288 | ||
Genetic analysis of the beta-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to beta-lactam antibiotics | Q45256213 | ||
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. | Q45947385 | ||
Determinants of the streptococcal surface glycoprotein GspB that facilitate export by the accessory Sec system. | Q45992753 | ||
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. | Q46008320 | ||
Targeting of unfolded PhoA to the TAT translocon of Escherichia coli | Q46786492 | ||
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. | Q52513940 | ||
The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism. | Q53410084 | ||
Bacterial sec-translocase unfolds and translocates a class of folded protein domains. | Q54437009 | ||
The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli | Q57839654 | ||
Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli | Q67898246 | ||
Lipoprotein antigens of Mycobacterium tuberculosis | Q67992293 | ||
Genetic methods for deciphering virulence determinants of Mycobacterium tuberculosis | Q78635273 | ||
P433 | issue | 4 | |
P407 | language of work or name | English | Q1860 |
P1104 | number of pages | 10 | |
P304 | page(s) | 672-681 | |
P577 | publication date | 2012-11-30 | |
P1433 | published in | Journal of Bacteriology | Q478419 |
P1476 | title | Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain | |
P478 | volume | 195 |
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Q36575070 | Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2. |
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Q64887171 | The Two Distinct Types of SecA2-Dependent Export Systems. |
Q48250974 | The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY. |
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