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Items: 1 to 20 of 119

1.

From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins.

Ogura T, Matsushita-Ishiodori Y, Johjima A, Nishizono M, Nishikori S, Esaki M, Yamanaka K.

Biochem Soc Trans. 2008 Feb;36(Pt 1):68-71. doi: 10.1042/BST0360068.

PMID:
18208388
2.

Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis.

Yamada-Inagawa T, Okuno T, Karata K, Yamanaka K, Ogura T.

J Biol Chem. 2003 Dec 12;278(50):50182-7. Epub 2003 Sep 26.

3.

Characterization of mutants of the Escherichia coli AAA protease, FtsH, carrying a mutation in the central pore region.

Okuno T, Yamanaka K, Ogura T.

J Struct Biol. 2006 Oct;156(1):109-14. Epub 2006 Mar 6.

PMID:
16563799
4.

Substrate specific consequences of central pore mutations in the i-AAA protease Yme1 on substrate engagement.

Graef M, Langer T.

J Struct Biol. 2006 Oct;156(1):101-8. Epub 2006 Feb 21.

PMID:
16527490
5.

Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severing.

Matsushita-Ishiodori Y, Yamanaka K, Hashimoto H, Esaki M, Ogura T.

Genes Cells. 2009 Aug;14(8):925-40. doi: 10.1111/j.1365-2443.2009.01320.x. Epub 2009 Jul 13.

6.

Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase.

Park E, Rho YM, Koh OJ, Ahn SW, Seong IS, Song JJ, Bang O, Seol JH, Wang J, Eom SH, Chung CH.

J Biol Chem. 2005 Jun 17;280(24):22892-8. Epub 2005 Apr 22.

7.
8.

Common and specific mechanisms of AAA+ proteins involved in protein quality control.

Mogk A, Haslberger T, Tessarz P, Bukau B.

Biochem Soc Trans. 2008 Feb;36(Pt 1):120-5. doi: 10.1042/BST0360120. Review.

PMID:
18208398
9.

Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease.

Leonhard K, Stiegler A, Neupert W, Langer T.

Nature. 1999 Mar 25;398(6725):348-51.

PMID:
10192337
10.

An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases.

Augustin S, Gerdes F, Lee S, Tsai FT, Langer T, Tatsuta T.

Mol Cell. 2009 Sep 11;35(5):574-85. doi: 10.1016/j.molcel.2009.07.018.

11.

AAA+ ATPases: achieving diversity of function with conserved machinery.

White SR, Lauring B.

Traffic. 2007 Dec;8(12):1657-67. Epub 2007 Sep 26. Review.

12.
13.

Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding.

Erbse AH, Wagner JN, Truscott KN, Spall SK, Kirstein J, Zeth K, Turgay K, Mogk A, Bukau B, Dougan DA.

FEBS J. 2008 Apr;275(7):1400-10. doi: 10.1111/j.1742-4658.2008.06304.x. Epub 2008 Feb 14.

14.

Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein.

Wang Q, Song C, Irizarry L, Dai R, Zhang X, Li CC.

J Biol Chem. 2005 Dec 9;280(49):40515-23. Epub 2005 Oct 10.

15.

VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase.

Gerega A, Rockel B, Peters J, Tamura T, Baumeister W, Zwickl P.

J Biol Chem. 2005 Dec 30;280(52):42856-62. Epub 2005 Oct 19.

16.

[Structure, function and mechanisms of action of ATPases from the AAA superfamily of proteins].

Kedzierska S.

Postepy Biochem. 2006;52(3):330-8. Review. Polish.

PMID:
17201069
17.

The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubules.

Matsushita-Ishiodori Y, Yamanaka K, Ogura T.

Biochem Biophys Res Commun. 2007 Jul 20;359(1):157-62. Epub 2007 May 22.

PMID:
17531954
18.

The exceptionally tight affinity of DnaA for ATP/ADP requires a unique aspartic acid residue in the AAA+ sensor 1 motif.

Kawakami H, Ozaki S, Suzuki S, Nakamura K, Senriuchi T, Su'etsugu M, Fujimitsu K, Katayama T.

Mol Microbiol. 2006 Dec;62(5):1310-24. Epub 2006 Oct 17.

19.

A conserved unfoldase activity for the p97 AAA-ATPase in proteasomal degradation.

Beskow A, Grimberg KB, Bott LC, Salomons FA, Dantuma NP, Young P.

J Mol Biol. 2009 Dec 11;394(4):732-46. doi: 10.1016/j.jmb.2009.09.050. Epub 2009 Sep 24.

PMID:
19782090
20.

The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation.

Bieniossek C, Niederhauser B, Baumann UM.

Proc Natl Acad Sci U S A. 2009 Dec 22;106(51):21579-84. doi: 10.1073/pnas.0910708106. Epub 2009 Dec 2.

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