These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Journal Abstract Search
226 related items for PubMed ID: 7968527
1. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mitchell C, Oliver D. Mol Microbiol; 1993 Nov; 10(3):483-97. PubMed ID: 7968527 [Abstract] [Full Text] [Related]
2. Integration of SecA protein into the Escherichia coli inner membrane is regulated by its amino-terminal ATP-binding domain. Rajapandi T, Oliver D. Mol Microbiol; 1996 Apr; 20(1):43-51. PubMed ID: 8861203 [Abstract] [Full Text] [Related]
3. Characterization of a potential catalytic residue, Asp-133, in the high affinity ATP-binding site of Escherichia coli SecA, translocation ATPase. Sato K, Mori H, Yoshida M, Mizushima S. J Biol Chem; 1996 Jul 19; 271(29):17439-44. PubMed ID: 8663354 [Abstract] [Full Text] [Related]
5. Identification of the magnesium-binding domain of the high-affinity ATP-binding site of the Bacillus subtilis and Escherichia coli SecA protein. van der Wolk JP, Klose M, de Wit JG, den Blaauwen T, Freudl R, Driessen AJ. J Biol Chem; 1995 Aug 11; 270(32):18975-82. PubMed ID: 7642557 [Abstract] [Full Text] [Related]
6. Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo. Klose M, Schimz KL, van der Wolk J, Driessen AJ, Freudl R. J Biol Chem; 1993 Feb 25; 268(6):4504-10. PubMed ID: 8440733 [Abstract] [Full Text] [Related]
7. Characterization of a Bacillus subtilis SecA mutant protein deficient in translocation ATPase and release from the membrane. van der Wolk J, Klose M, Breukink E, Demel RA, de Kruijff B, Freudl R, Driessen AJ. Mol Microbiol; 1993 Apr 25; 8(1):31-42. PubMed ID: 8497195 [Abstract] [Full Text] [Related]
9. Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function. Sianidis G, Karamanou S, Vrontou E, Boulias K, Repanas K, Kyrpides N, Politou AS, Economou A. EMBO J; 2001 Mar 01; 20(5):961-70. PubMed ID: 11230120 [Abstract] [Full Text] [Related]
10. Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding. Ramamurthy V, Oliver D. J Biol Chem; 1997 Sep 12; 272(37):23239-46. PubMed ID: 9287332 [Abstract] [Full Text] [Related]
11. The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events. van der Wolk JP, de Wit JG, Driessen AJ. EMBO J; 1997 Dec 15; 16(24):7297-304. PubMed ID: 9405359 [Abstract] [Full Text] [Related]
14. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J. Science; 2002 Sep 20; 297(5589):2018-26. PubMed ID: 12242434 [Abstract] [Full Text] [Related]
15. Identification of export proteins from Mycobacterium tuberculosis that interact with SecA. Owens MU, Schmidt MG, King CH, Quinn FD. Ann N Y Acad Sci; 1996 Oct 25; 797():240-1. PubMed ID: 8993366 [No Abstract] [Full Text] [Related]
16. Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase. Dapic V, Oliver D. J Biol Chem; 2000 Aug 11; 275(32):25000-7. PubMed ID: 10835419 [Abstract] [Full Text] [Related]
19. Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Mori H, Sugiyama H, Yamanaka M, Sato K, Tagaya M, Mizushima S. J Biochem; 1998 Jul 11; 124(1):122-9. PubMed ID: 9644254 [Abstract] [Full Text] [Related]
20. Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation. Schmidt MO, Brosh RM, Oliver DB. J Biol Chem; 2001 Oct 05; 276(40):37076-85. PubMed ID: 11477104 [Abstract] [Full Text] [Related] Page: [Next] [New Search]