| scholarly article | Q13442814 |
| P50 | author | Shashi Bhushan | Q42458926 |
| Joen Luirink | Q55137375 | ||
| Vikram B Kasaragod | Q61314221 | ||
| P2093 | author name string | Thorsten Mielke | |
| Joen Luirink | |||
| Jörg Bürger | |||
| Jochen Kuper | |||
| Rajkumar Singh | |||
| Rahul Jaiswal | |||
| Christian Kraft | |||
| Kushal Sejwal | |||
| P2860 | cites work | The SWISS-MODEL Repository and associated resources | Q24656047 |
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| Molecular mechanism and structure of Trigger Factor bound to the translating ribosome | Q27650662 | ||
| Structure of a complex of the ATPase SecA and the protein-translocation channel | Q27652526 | ||
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| SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity | Q28740702 | ||
| Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research | Q29619122 | ||
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| A large conformational change of the translocation ATPase SecA | Q30776655 | ||
| SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase center | Q33803719 | ||
| Dimeric SecA is essential for protein translocation | Q33836404 | ||
| Probing the affinity of SecA for signal peptide in different environments | Q34979875 | ||
| Selective photoaffinity labeling identifies the signal peptide binding domain on SecA | Q35750297 | ||
| The bacterial Sec-translocase: structure and mechanism. | Q35814696 | ||
| A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation | Q36414988 | ||
| Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex | Q36455887 | ||
| Complex behavior in solution of homodimeric SecA. | Q36639172 | ||
| The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins | Q37506110 | ||
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| Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes | Q37973762 | ||
| Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane | Q39647998 | ||
| Regulation of the Escherichia coli secA gene by protein secretion defects: analysis of secA, secB, secD, and secY mutants | Q39953808 | ||
| Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion | Q40082687 | ||
| SecA dimer cross-linked at its subunit interface is functional for protein translocation | Q40724558 | ||
| Structure of the E. coli signal recognition particle bound to a translating ribosome. | Q41625398 | ||
| Mapping of the SecA·SecY and SecA·SecG Interfaces by Site-directed in Vivo Photocross-linking | Q41832626 | ||
| Identification of the preprotein binding domain of SecA. | Q42485674 | ||
| Competitive binding of the SecA ATPase and ribosomes to the SecYEG translocon. | Q42558513 | ||
| Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer. | Q42601546 | ||
| A role for the two-helix finger of the SecA ATPase in protein translocation. | Q43181763 | ||
| The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules | Q44946841 | ||
| Covalently dimerized SecA is functional in protein translocation | Q46663736 | ||
| Escherichia coli membranes depleted of SecYEG elicit SecA-dependent ion-channel activity but lose signal peptide specificity | Q48642879 | ||
| Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: purification, crystallization and structure determination | Q49203495 | ||
| Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export | Q52563568 | ||
| SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria | Q52607663 | ||
| 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 | ||
| Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel | Q54443529 | ||
| Selective SecA association with signal sequences in ribosome-bound nascent chains: a potential role for SecA in ribosome targeting to the bacterial membrane. | Q54480226 | ||
| Escherichia coli SecA truncated at its termini is functional and dimeric. | Q54491433 | ||
| Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. | Q54535975 | ||
| SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer. | Q54646917 | ||
| SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer. | Q54701776 | ||
| Quaternary Structure of SecA in Solution and Bound to SecYEG Probed at the Single Molecule Level | Q63359798 | ||
| A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA | Q80310735 | ||
| P433 | issue | 10 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | protein structure | Q735188 |
| P304 | page(s) | 7190-7199 | |
| P577 | publication date | 2014-01-17 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome | |
| P478 | volume | 289 |
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| Q46316930 | SecA mediates cotranslational targeting and translocation of an inner membrane protein |
| Q40259224 | SecA-a New Twist in the Tale |
| Q58751987 | Structures of Mycobacterium smegmatis 70S ribosomes in complex with HPF, tmRNA, and P-tRNA |
| Q57463329 | Substrate Proteins Take Shape at an Improved Bacterial Translocon |
| Q83231326 | The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity |
| Q90391222 | The molecular mechanism of cotranslational membrane protein recognition and targeting by SecA |
| Q54201374 | The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria |
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