scholarly article | Q13442814 |
P2093 | author name string | Linda L Randall | |
Jennine M Crane | |||
P2860 | cites work | A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB | Q73138769 |
The high affinity ATP binding site modulates the SecA-precursor interaction | Q73276020 | ||
Evidence that SecB enhances the activity of SecA | Q73738765 | ||
Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions | Q73783901 | ||
A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secB | Q73905825 | ||
Expression of gpsA encoding biosynthetic sn-glycerol 3-phosphate dehydrogenase suppresses both the LB- phenotype of a secB null mutant and the cold-sensitive phenotype of a secG null mutant | Q74027915 | ||
The phase property of membrane phospholipids is affected by the functionality of signal peptides from the Escherichia coli ribose-binding protein | Q74066173 | ||
YidC mediates membrane protein insertion in bacteria | Q74191988 | ||
SecA folds via a dimeric intermediate | Q74337250 | ||
Tyr-326 plays a critical role in controlling SecA-preprotein interaction | Q74347195 | ||
PROTEIN SYNTHESIS BY POLYRIBOSOMES ON PROTOPLAST MEMBRANES OF B. MEGATERIUM | Q76606257 | ||
ON THE CYTOLOGICAL UNIT FOR PROTEIN SYNTHESIS IN VIVO IN E. COLI. II. STUDIES WITH INTACT CELLS OF TYPE B | Q76850072 | ||
Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers | Q77927053 | ||
A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA | Q80310735 | ||
Determining the conductance of the SecY protein translocation channel for small molecules | Q80390141 | ||
Structure of the E. coli protein-conducting channel bound to a translating ribosome | Q24539141 | ||
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation | Q24596484 | ||
Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB | Q24618046 | ||
Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences | Q24644640 | ||
Preprotein-controlled catalysis in the helicase motor of SecA | Q24670723 | ||
Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma | Q24681545 | ||
Assembly and structure of the T3SS | Q26865556 | ||
A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and function | Q26995227 | ||
Structure and mechanism of Escherichia coli type I signal peptidase | Q26999911 | ||
YidC/Alb3/Oxa1 Family of Insertases | Q27025116 | ||
Crystal structure of the bacterial protein export chaperone secB | Q27628763 | ||
Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii | Q27629461 | ||
Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism | Q27636769 | ||
Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA | Q27639672 | ||
Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase | Q27640590 | ||
Structural determinants of SecB recognition by SecA in bacterial protein translocation | Q27642253 | ||
Crystal structure of SecB from Escherichia coli | Q27642641 | ||
X-ray structure of a protein-conducting channel | Q27642744 | ||
Structure of dimeric SecA, the Escherichia coli preprotein translocase motor | Q27643567 | ||
Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR | Q27649095 | ||
Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist | Q27649284 | ||
Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC | Q27649371 | ||
Ribosome binding of a single copy of the SecY complex: implications for protein translocation | Q27649425 | ||
Crystal structure of a bacterial signal Peptide peptidase | Q27649465 | ||
The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft | Q27649739 | ||
Analysis of the isolated SecA DEAD motor suggests a mechanism for chemical-mechanical coupling | Q27651892 | ||
Structure of a complex of the ATPase SecA and the protein-translocation channel | Q27652526 | ||
Conformational transition of Sec machinery inferred from bacterial SecYE structures | Q27652527 | ||
Crystallographic analysis of bacterial signal peptidase in ternary complex with arylomycin A2 and a beta-sultam inhibitor | Q27656899 | ||
Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA | Q27657911 | ||
Regulation of the Protein-Conducting Channel by a Bound Ribosome | Q27658163 | ||
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes | Q27664605 | ||
Cryo-EM structure of the ribosome–SecYE complex in the membrane environment | Q27667539 | ||
Protein transport by the bacterial Tat pathway | Q38192369 | ||
Architecture and assembly of the Type VI secretion system. | Q38200408 | ||
The Sec translocon mediated protein transport in prokaryotes and eukaryotes. | Q38206834 | ||
Fidelity of cotranslational protein targeting by the signal recognition particle | Q38217500 | ||
Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB. | Q38291165 | ||
Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase | Q38314889 | ||
SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli | Q38322783 | ||
A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. | Q38336960 | ||
Characterization of a region in mature LamB protein that interacts with a component of the export machinery of Escherichia coli | Q38338625 | ||
Escherichia coli sec mutants accumulate a processed immature form of maltose-binding protein (MBP), a late-phase intermediate in MBP export | Q38338914 | ||
Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli. | Q38341113 | ||
The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein | Q38347439 | ||
Diverse effects of the MalE-LacZ hybrid protein on Escherichia coli cell physiology | Q38350783 | ||
E. coli mutant pleiotropically defective in the export of secreted proteins | Q38356083 | ||
Different exported proteins in E. coli show differences in the temporal mode of processing in vivo | Q38356214 | ||
Protein localization in E. coli: is there a common step in the secretion of periplasmic and outer-membrane proteins? | Q38356265 | ||
Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm | Q38357752 | ||
Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures | Q38365596 | ||
Viability of an Escherichia coli pgsA null mutant lacking detectable phosphatidylglycerol and cardiolipin | Q39498543 | ||
The SecA subunit of Escherichia coli preprotein translocase is exposed to the periplasm | Q39568449 | ||
Genetic studies on protein export in bacteria | Q39590426 | ||
Folded HasA inhibits its own secretion through its ABC exporter | Q39645637 | ||
Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane | Q39647998 | ||
The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporter | Q39702705 | ||
Influence of impaired chaperone or secretion function on SecB production in Escherichia coli | Q39843192 | ||
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase | Q39918354 | ||
SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane | Q39932560 | ||
Involvement of SecB, a chaperone, in the export of ribose-binding protein | Q39935707 | ||
Conformational dynamics of the plug domain of the SecYEG protein-conducting channel. | Q39935945 | ||
Determinants of the quantity of the stable SecY complex in the Escherichia coli cell | Q39938069 | ||
Regulation of the Escherichia coli secA gene by protein secretion defects: analysis of secA, secB, secD, and secY mutants | Q39953808 | ||
Transcriptional organization within an Escherichia coli cell division gene cluster: direction of transcription of the cell separation gene envA | Q39966114 | ||
Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion | Q40082687 | ||
Mechanism of incorporation of cell envelope proteins in Escherichia coli | Q40248345 | ||
BINDING OF RIBOSOMES TO CYTOPLASMIC RETICULUM OF BACILLUS MEGATERIUM. | Q40438491 | ||
A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli. | Q40456503 | ||
A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase | Q34346496 | ||
Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad | Q34356733 | ||
Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile. | Q34363960 | ||
Structural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy. | Q34442682 | ||
MPIase is a glycolipozyme essential for membrane protein integration | Q34509067 | ||
Elongation arrest by SecM via a cascade of ribosomal RNA rearrangements | Q34528562 | ||
How azide inhibits ATP hydrolysis by the F-ATPases. | Q34637621 | ||
YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase | Q34663216 | ||
Energetics of SecA dimerization | Q34761920 | ||
Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules | Q34977908 | ||
Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro | Q35018606 | ||
SecB, one small chaperone in the complex milieu of the cell | Q35021874 | ||
Extracellular labeling of nascent polypeptides traversing the membrane of Escherichia coli | Q35035545 | ||
Conformational variation of the translocon enhancing chaperone SecDF. | Q35076035 | ||
The translational regulatory function of SecM requires the precise timing of membrane targeting. | Q35098853 | ||
Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria | Q35170737 | ||
The basis of asymmetry in the SecA:SecB complex | Q35207949 | ||
Subunit dynamics in Escherichia coli preprotein translocase | Q35271076 | ||
Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB. | Q35582444 | ||
Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning | Q35587373 | ||
A single copy of SecYEG is sufficient for preprotein translocation | Q35591711 | ||
Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles | Q35610508 | ||
Escherichia coli SecB stimulates export without maintaining export competence of ribose-binding protein signal sequence mutants. | Q35614280 | ||
Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes | Q35619782 | ||
Control of SecA and SecM translation by protein secretion | Q35737959 | ||
Selective photoaffinity labeling identifies the signal peptide binding domain on SecA | Q35750297 | ||
Conformational Changes of the Clamp of the Protein Translocation ATPase SecA | Q35754823 | ||
The bacterial Sec-translocase: structure and mechanism. | Q35814696 | ||
Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase | Q35837206 | ||
Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli | Q35920818 | ||
Position-dependent effects of polylysine on Sec protein transport | Q35921553 | ||
One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery. | Q35926815 | ||
Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins | Q35962797 | ||
PrlA and PrlG suppressors reduce the requirement for signal sequence recognition | Q35975083 | ||
Structure and function of a membrane component SecDF that enhances protein export | Q27667802 | ||
Synthesis and Characterization of the Arylomycin Lipoglycopeptide Antibiotics and the Crystallographic Analysis of Their Complex with Signal Peptidase | Q27675041 | ||
ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase | Q27675185 | ||
Structure of the SecY channel during initiation of protein translocation | Q27680440 | ||
A structural model of the active ribosome-bound membrane protein insertase YidC | Q27684647 | ||
Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State | Q27702712 | ||
Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor | Q27766053 | ||
Effects of pre-protein overexpression on SecB synthesis in Escherichia coli | Q28140412 | ||
Three-dimensional structure of the bacterial protein-translocation complex SecYEG | Q28217206 | ||
Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro | Q28264700 | ||
Modulation of folding pathways of exported proteins by the leader sequence | Q28294571 | ||
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 | ||
Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function | Q28354455 | ||
Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channels | Q28535409 | ||
SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity | Q28740702 | ||
Patterns of amino acids near signal-sequence cleavage sites | Q29616542 | ||
Outer membrane lipoprotein biogenesis: Lol is not the end. | Q30152837 | ||
The Bam machine: a molecular cooper | Q30155481 | ||
Lipoprotein sorting in bacteria. | Q30155534 | ||
Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: evidence from site-directed mutagenesis and carbodiimide labeling | Q30268386 | ||
Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli. | Q30401105 | ||
SecA, the motor of the secretion machine, binds diverse partners on one interactive surface | Q30485740 | ||
Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling | Q30496200 | ||
Orientation of SecA and SecB in complex, derived from disulfide cross-linking | Q30497880 | ||
The oligomeric state and arrangement of the active bacterial translocon | Q30498189 | ||
A large conformational change of the translocation ATPase SecA | Q30776655 | ||
Substrate specificity of the SecB chaperone | Q30815173 | ||
A comprehensive database of verified experimental data on protein folding kinetics | Q30852309 | ||
Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium | Q31664450 | ||
Secretion monitor, SecM, undergoes self-translation arrest in the cytosol | Q31923120 | ||
SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA. | Q33562009 | ||
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli | Q33562047 | ||
Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. | Q47611174 | ||
Effects of nonlamellar-prone lipids on the ATPase activity of SecA bound to model membranes | Q47682273 | ||
Cell-Free Protein Synthesis: Effects of Age and State of Ribosomal Aggregation | Q47715200 | ||
Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes | Q47763987 | ||
Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. | Q47917595 | ||
Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol | Q48080100 | ||
Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope | Q48395760 | ||
Evidence for posttranslational translocation of beta-lactamase across the bacterial inner membrane. | Q50213210 | ||
Protein sizes and stoichiometry in the chaperone SecB--RBPTI complex estimated by ANS fluorescence. | Q50524678 | ||
Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB. | Q50759209 | ||
The long alpha-helix of SecA is important for the ATPase coupling of translocation. | Q51127253 | ||
SecA protein is required for secretory protein translocation into E. coli membrane vesicles. | Q52455868 | ||
Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane. | Q52457501 | ||
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. | Q52513940 | ||
Zinc stabilizes the SecB binding site of SecA. | Q52534778 | ||
The role of the conserved box E residues in the active site of the Escherichia coli type I signal peptidase. | Q52538173 | ||
Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. | Q52563568 | ||
Measurement of intracellular sodium concentration and sodium transport in Escherichia coli by 23Na nuclear magnetic resonance. | Q52645070 | ||
Characterization of the annular lipid shell of the Sec translocon. | Q53446395 | ||
Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. | Q54154827 | ||
Reconstitution of functionally efficient SecA-dependent protein-conducting channels: transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels. | Q54318600 | ||
In vitro analysis of the process of translocation of OmpA across the Escherichia coli cytoplasmic membrane. A translocation intermediate accumulates transiently in the absence of the proton motive force. | Q54340916 | ||
Conformational changes of the chaperone SecB upon binding to a model substrate--bovine pancreatic trypsin inhibitor (BPTI). | Q54354833 | ||
Expression, purification and characterization of the Escherichia coli integral membrane protein YajC. | Q54372106 | ||
Systematic analysis of native membrane protein complexes in Escherichia coli. | Q54372766 | ||
Expression and purification of the recombinant membrane protein YidC: a case study for increased stability and solubility. | Q54420417 | ||
The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon. | Q54423305 | ||
Topology inversion of SecG is essential for cytosolic SecA-dependent stimulation of protein translocation. | Q54436102 | ||
Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. | Q54443529 | ||
Allosteric regulation of SecA: magnesium-mediated control of conformation and activity. | Q54443615 | ||
Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity. | Q54452792 | ||
Defining the role of the Escherichia coli chaperone SecB using comparative proteomics. | Q54473734 | ||
NMR structure of the C-terminal domain of SecA in the free state. | Q54497650 | ||
Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. | Q54535975 | ||
Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR. | Q54536175 | ||
SecDFyajC forms a heterotetrameric complex with YidC. | Q54543620 | ||
Targeting, insertion, and localization of Escherichia coli YidC. | Q54551389 | ||
Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding. | Q54559159 | ||
Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands. | Q54561671 | ||
Identification of a region of interaction between Escherichia coli SecA and SecY proteins. | Q54567468 | ||
Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase. | Q54567779 | ||
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 | ||
Different PrlA proteins increase the efficiency of periplasmic production of human interleukin-6 in Escherichia coli. | Q54582761 | ||
SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature. | Q54593351 | ||
SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. | Q54598039 | ||
Mapping of the Binding Frame for the Chaperone SecB within a Natural Ligand, Galactose-binding Protein | Q54601274 | ||
A quantitative assay to determine the amount of signal peptidase I in E. coli and the orientation of membrane vesicles. | Q54602070 | ||
The C terminus of SecA is involved in both lipid binding and SecB binding. | Q54614038 | ||
Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo. | Q54633342 | ||
Membrane vesicles containing overproduced SecY and SecE exhibit high translocation ATPase activity and countermovement of protons in a SecA- and presecretory protein-dependent manner. | Q54658915 | ||
Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo | Q36098016 | ||
Accumulation of secretory protein precursors in Escherichia coli induces the heat shock response | Q36102319 | ||
Genetic and molecular characterization of the Escherichia coli secD operon and its products | Q36105112 | ||
Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli | Q36123480 | ||
Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3 | Q36150427 | ||
Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria. | Q36155063 | ||
Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon | Q36159495 | ||
The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro | Q36164926 | ||
The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export. | Q36174105 | ||
Bacterial protein translocation requires only one copy of the SecY complex in vivo | Q36205340 | ||
Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis | Q36215035 | ||
secD, a new gene involved in protein export in Escherichia coli | Q36231634 | ||
Suppression of a signal sequence mutation by an amino acid substitution in the mature portion of the maltose-binding protein | Q36234894 | ||
Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coli | Q36253218 | ||
Determination of the binding frame within a physiological ligand for the chaperone SecB. | Q36278522 | ||
Interaction of SecB with intermediates along the folding pathway of maltose-binding protein | Q36279244 | ||
Electrospray mass spectrometric investigation of the chaperone SecB. | Q36279705 | ||
Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein | Q36280530 | ||
The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding | Q36280717 | ||
Calorimetric analyses of the interaction between SecB and its ligands | Q36280993 | ||
Proper interaction between at least two components is required for efficient export of proteins to the Escherichia coli cell envelope | Q36289283 | ||
Post-translational modification and processing of Escherichia coli prolipoprotein in vitro | Q36289591 | ||
Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. | Q36321596 | ||
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli | Q36326983 | ||
Evidence for specificity at an early step in protein export in Escherichia coli | Q36361933 | ||
Role for membrane potential in the secretion of protein into the periplasm of Escherichia coli | Q36366860 | ||
Isolation of the Escherichia coli leader peptidase gene and effects of leader peptidase overproduction in vivo | Q36373675 | ||
Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli | Q36390365 | ||
Cation transport in Escherichia coli. VIII. Potassium transport mutants | Q36407638 | ||
Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex | Q36455887 | ||
Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2. | Q36575070 | ||
Complex behavior in solution of homodimeric SecA. | Q36639172 | ||
Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking | Q36674746 | ||
High selectivity with low specificity: how SecB has solved the paradox of chaperone binding | Q40497588 | ||
Nucleotide and Phospholipid-Dependent Control of PPXD and C-Domain Association for SecA ATPase | Q40549080 | ||
A new form of structural lipoprotein of outer membrane of Escherichia coli | Q40757311 | ||
Precursors of major outer membrane proteins of Escherichia coli | Q40807978 | ||
Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli | Q40820187 | ||
The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. | Q41006640 | ||
Induction of non-bilayer lipid structures by functional signal peptides | Q41204756 | ||
The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor | Q41219838 | ||
Synthesis of Exported Proteins by Membrane-Bound Polysomes from Escherichia coli | Q41259974 | ||
DCCD inhibits protein translocation into plasma membrane vesicles from Escherichia coli at two different steps | Q41357977 | ||
Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linking | Q41445854 | ||
The requirement for energy during export of beta-lactamase in Escherichia coli is fulfilled by the total protonmotive force | Q41569479 | ||
Inactivation of protein translocation by cold-sensitive mutations in the yajC-secDF operon | Q41820715 | ||
Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli | Q41827408 | ||
Requirements for substrate recognition by bacterial leader peptidase | Q41843667 | ||
The dynamic action of SecA during the initiation of protein translocation. | Q41855262 | ||
Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands | Q41866614 | ||
SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study | Q41897858 | ||
Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export | Q41904736 | ||
Protein synthesis by membrane-bound and free ribosomes of secretory and non-secretory tissues | Q41906977 | ||
Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins | Q41960890 | ||
Structure of the SecY complex unlocked by a preprotein mimic. | Q42000002 | ||
Tryptophan fluorescence study on the interaction of the signal peptide of the Escherichia coli outer membrane protein PhoE with model membranes | Q42006855 | ||
Topologically fixed SecG is fully functional | Q42073427 | ||
Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA | Q42078600 | ||
YfgM is an ancillary subunit of the SecYEG translocon in Escherichia coli | Q42087433 | ||
The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release | Q42152267 | ||
Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase. | Q42177840 | ||
Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation | Q42213460 | ||
Identification of the preprotein binding domain of SecA. | Q42485674 | ||
Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer. | Q42601546 | ||
The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal | Q42621979 | ||
Prolyl-tRNA(Pro) in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA. | Q42640310 | ||
Characterization of the Escherichia coli protein-export gene secB. | Q42644465 | ||
Ion conductivity of the bacterial translocation channel SecYEG engaged in translocation | Q42850306 | ||
The secD locus of E. coli codes for two membrane proteins required for protein export | Q42927284 | ||
Sites of interaction between SecA and the chaperone SecB, two proteins involved in export | Q43095210 | ||
A role for the two-helix finger of the SecA ATPase in protein translocation. | Q43181763 | ||
Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB. | Q43265896 | ||
Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli | Q43424522 | ||
SecB-mediated protein export need not occur via kinetic partitioning | Q43527176 | ||
Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB. | Q43660562 | ||
Differential expression of secretion machinery during bacterial growth: SecY and SecF decrease while SecA increases during transition from exponential phase to stationary phase | Q43661432 | ||
Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidase | Q43754168 | ||
SecDFyajC is not required for the maintenance of the proton motive force | Q43798449 | ||
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes | Q43822332 | ||
Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system. | Q43895294 | ||
Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization | Q43907653 | ||
Suppressor mutations that restore export of a protein with a defective signal sequence | Q43987617 | ||
Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA. | Q44163723 | ||
Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate | Q44493487 | ||
Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interaction | Q44560492 | ||
The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins | Q44686930 | ||
Regulation of signal peptidase by phospholipids in membrane: characterization of phospholipid bilayer incorporated Escherichia coli signal peptidase | Q44713919 | ||
Alteration of the phospholipid composition of Escherichia coli through genetic manipulation | Q44807226 | ||
Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor | Q44891154 | ||
Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state | Q44925080 | ||
Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm | Q44976888 | ||
Solution NMR structure and X-ray absorption analysis of the C-terminal zinc-binding domain of the SecA ATPase | Q44983734 | ||
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. | Q46008320 | ||
Effect of crowding agents, signal peptide, and chaperone SecB on the folding and aggregation of E. coli maltose binding protein. | Q46055337 | ||
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 | ||
The oligomeric distribution of SecYEG is altered by SecA and translocation ligands | Q46768434 | ||
Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro | Q33577044 | ||
Mobility of cytoplasmic, membrane, and DNA-binding proteins in Escherichia coli | Q33647888 | ||
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 | ||
Identification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms. | Q33723631 | ||
Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo | Q33726768 | ||
Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon | Q33737540 | ||
Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer | Q33773458 | ||
Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression | Q33787527 | ||
SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase center | Q33803719 | ||
High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein | Q33820929 | ||
SecM facilitates translocase function of SecA by localizing its biosynthesis | Q33848928 | ||
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 | ||
The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter. | Q33888292 | ||
PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation | Q33889035 | ||
The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits | Q33891061 | ||
The secD locus of E.coli codes for two membrane proteins required for protein export | Q33922088 | ||
The action of cardiolipin on the bacterial translocon. | Q33933121 | ||
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. | Q33939397 | ||
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene. | Q33953915 | ||
Precursors of three exported proteins in Escherichia coli | Q33966426 | ||
Dynamic interaction of the sec translocon with the chaperone PpiD | Q33985391 | ||
Catabolic repression of secB expression is positively controlled by cyclic AMP (cAMP) receptor protein-cAMP complexes at the transcriptional level | Q33991514 | ||
A signal sequence is not required for protein export in prlA mutants of Escherichia coli | Q34044995 | ||
PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains | Q34058568 | ||
A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli. | Q34058655 | ||
The ribosomal exit tunnel functions as a discriminating gate | Q34118341 | ||
Degradation of a signal peptide by protease IV and oligopeptidase A. | Q34164260 | ||
Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation | Q34309801 | ||
Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein | Q34322460 | ||
SecB is a bona fide generalized chaperone in Escherichia coli | Q34336036 | ||
FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit | Q34342148 | ||
Localization of Polyribosomes Containing Alkaline Phosphatase Nascent Polypeptides on Membranes of Escherichia coli | Q36768647 | ||
Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini | Q36769544 | ||
Protein secretion and membrane insertion systems in gram-negative bacteria | Q36839222 | ||
prl mutations in the Escherichia coli secG gene | Q36844982 | ||
Crystal structure of a substrate-engaged SecY protein-translocation channel | Q36865827 | ||
Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations. | Q36910150 | ||
Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation | Q36932458 | ||
Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer | Q36942421 | ||
Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer | Q37029669 | ||
Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species | Q37031742 | ||
Translocon “Pulling” of Nascent SecM Controls the Duration of Its Translational Pause and Secretion-Responsive secA Regulation | Q37051988 | ||
Energy transduction in protein transport and the ATP hydrolytic cycle of SecA | Q37122860 | ||
The lateral gate of SecYEG opens during protein translocation | Q37257359 | ||
Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study | Q37369897 | ||
Mapping polypeptide interactions of the SecA ATPase during translocation | Q37428012 | ||
Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocase | Q37445539 | ||
ATP is essential for protein translocation into Escherichia coli membrane vesicles | Q37522633 | ||
Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli | Q37557649 | ||
prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors | Q37564839 | ||
In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli | Q37578783 | ||
Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein | Q37595620 | ||
SecD and SecF facilitate protein export in Escherichia coli. | Q37628246 | ||
Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC. | Q37687646 | ||
The signal peptide | Q37942677 | ||
Biophysical studies of signal peptides: implications for signal sequence functions and the involvement of lipid in protein export | Q37949458 | ||
The twin-arginine translocation (Tat) protein export pathway | Q38017546 | ||
The Type 1 secretion pathway - the hemolysin system and beyond | Q38152930 | ||
Type V secretion: from biogenesis to biotechnology | Q38165623 | ||
Mechanism and structure of the bacterial type IV secretion systems | Q38175753 | ||
Type II secretion system: a magic beanstalk or a protein escalator | Q38175754 | ||
The membrane insertase YidC. | Q38177989 | ||
Co-translational protein targeting to the bacterial membrane | Q38186912 | ||
SecA-mediated targeting and translocation of secretory proteins. | Q38192370 | ||
Synthesis and Transfer of Amylase in Pigeon Pancreatic Microsomes | Q72838986 | ||
The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme | Q72932795 | ||
Maturation of exported proteins in Escherichia coli. Requirement for energy, site and kinetics of processing | Q72939872 | ||
Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein. | Q54663164 | ||
Identification of potential active-site residues in the Escherichia coli leader peptidase | Q54676180 | ||
DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli | Q54676319 | ||
Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein | Q54682002 | ||
Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli. | Q54695475 | ||
Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membranes. | Q54696892 | ||
New suppressors of signal-sequence mutations, prlG, are linked tightly to the secE gene of Escherichia coli. | Q54727879 | ||
Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. | Q54738841 | ||
Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein. | Q54740268 | ||
A functional decaisoleucine-containing signal sequence. Construction by cassette mutagenesis. | Q54748298 | ||
Coupling between the sodium and proton gradients in respiring Escherichia coli cells measured by 23Na and 31P nuclear magnetic resonance. | Q54779208 | ||
Atomic Model of the E.coli Membrane-bound Protein Translocation Complex SecYEG | Q57840346 | ||
Disorder-order folding transitions underlie catalysis in the helicase motor of SecA | Q57976550 | ||
A molecular switch in SecA protein couples ATP hydrolysis to protein translocation | Q57976571 | ||
Separable ATPase and Membrane Insertion Domains of the SecA Subunit of Preprotein Translocase | Q57976575 | ||
Non-bilayer Lipids Stimulate the Activity of the Reconstituted Bacterial Protein Translocase | Q63359870 | ||
Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA | Q63359903 | ||
Interaction of SecB with soluble SecA 1 | Q63359914 | ||
Anionic phospholipids are essential for alpha-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles | Q67486006 | ||
Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli | Q67898246 | ||
Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding | Q67901010 | ||
A peptide corresponding to an export-defective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranes | Q67926674 | ||
Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function | Q68030460 | ||
Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo | Q68072417 | ||
The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli | Q68079685 | ||
Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative Structure | Q68208733 | ||
In vitro protein translocation into inverted membrane vesicles prepared from Vibrio alginolyticus is stimulated by the electrochemical potential of Na+ in the presence of Escherichia coli SecA | Q68459374 | ||
No specific recognition of leader peptide by SecB, a chaperone involved in protein export | Q68512094 | ||
SecE-dependent overproduction of SecY in Escherichia coli. Evidence for interaction between two components of the secretory machinery | Q68534743 | ||
SecB protein stabilizes a translocation-competent state of purified prePhoE protein | Q69360855 | ||
SecA protein is directly involved in protein secretion in Escherichia coli | Q69484198 | ||
Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation system | Q69484332 | ||
Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties | Q69542568 | ||
In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factor | Q70137148 | ||
Energy is required for maturation of exported proteins in Escherichia coli | Q70159788 | ||
In vitro translocation of protein across Escherichia coli membrane vesicles requires both the proton motive force and ATP | Q70166275 | ||
The biosynthesis of membrane-bound M13 coat protein. Energetics and assembly intermediates | Q70232037 | ||
A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins | Q70244970 | ||
Energetics and intermediates of the assembly of Protein OmpA into the outer membrane of Escherichia coli | Q70246320 | ||
Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation | Q70373251 | ||
Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation | Q71056385 | ||
Polysomes Extracted from Escherichia coli by Freeze-Thaw-Lysozyme Lysis | Q71189776 | ||
Regulation of a membrane component required for protein secretion in Escherichia coli | Q71444140 | ||
Purification and characterization of leader (signal) peptidase from Escherichia coli | Q72144849 | ||
Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12) | Q72196641 | ||
Identification of the secY (prlA) gene product involved in protein export in Escherichia coli | Q72409380 | ||
Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coli | Q72800486 | ||
P433 | issue | 2 | |
P921 | main subject | Escherichia coli | Q25419 |
P577 | publication date | 2017-11-01 | |
P1433 | published in | EcoSal Plus | Q27725548 |
P1476 | title | The Sec System: Protein Export in Escherichia coli | |
P478 | volume | 7 |
Q91892843 | Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion |
Q57056828 | Co-assembly of SecYEG and SecA fully restores the properties of the native translocon |
Q64898340 | Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers. |
Q92510993 | Enhancing Recombinant Protein Yields in the E. coli Periplasm by Combining Signal Peptide and Production Rate Screening |
Q89737499 | Escherichia coli Can Adapt Its Protein Translocation Machinery for Enhanced Periplasmic Recombinant Protein Production |
Q91704513 | Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region |
Q92867260 | Inner Membrane Translocases and Insertases |
Q92601530 | Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome |
Q58569559 | Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis |
Q57463329 | Substrate Proteins Take Shape at an Improved Bacterial Translocon |
Q64887171 | The Two Distinct Types of SecA2-Dependent Export Systems. |
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