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Items: 1 to 20 of 116

1.

A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments.

Pires R, Hartlieb B, Signor L, Schoehn G, Lata S, Roessle M, Moriscot C, Popov S, Hinz A, Jamin M, Boyer V, Sadoul R, Forest E, Svergun DI, Göttlinger HG, Weissenhorn W.

Structure. 2009 Jun 10;17(6):843-56. doi: 10.1016/j.str.2009.04.007.

2.

ALIX-CHMP4 interactions in the human ESCRT pathway.

McCullough J, Fisher RD, Whitby FG, Sundquist WI, Hill CP.

Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7687-91. doi: 10.1073/pnas.0801567105. Epub 2008 May 29.

3.

Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding.

Fisher RD, Chung HY, Zhai Q, Robinson H, Sundquist WI, Hill CP.

Cell. 2007 Mar 9;128(5):841-52.

4.

Structure of the Bro1 domain protein BROX and functional analyses of the ALIX Bro1 domain in HIV-1 budding.

Zhai Q, Landesman MB, Robinson H, Sundquist WI, Hill CP.

PLoS One. 2011;6(12):e27466. doi: 10.1371/journal.pone.0027466. Epub 2011 Dec 5.

5.

Activation of the retroviral budding factor ALIX.

Zhai Q, Landesman MB, Chung HY, Dierkers A, Jeffries CM, Trewhella J, Hill CP, Sundquist WI.

J Virol. 2011 Sep;85(17):9222-6. doi: 10.1128/JVI.02653-10. Epub 2011 Jun 29.

6.
7.

Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis.

Morita E, Sandrin V, Chung HY, Morham SG, Gygi SP, Rodesch CK, Sundquist WI.

EMBO J. 2007 Oct 3;26(19):4215-27. Epub 2007 Sep 13. Erratum in: EMBO J. 2012 Jul 18;31(14):3228.

8.

Decoding the intrinsic mechanism that prohibits ALIX interaction with ESCRT and viral proteins.

Zhou X, Si J, Corvera J, Gallick GE, Kuang J.

Biochem J. 2010 Dec 15;432(3):525-34. doi: 10.1042/BJ20100862.

9.

The CHMP4b- and Src-docking sites in the Bro1 domain are autoinhibited in the native state of Alix.

Zhou X, Pan S, Sun L, Corvera J, Lee YC, Lin SH, Kuang J.

Biochem J. 2009 Mar 1;418(2):277-84. doi: 10.1042/BJ20081388.

PMID:
19016654
10.

Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55.

Lee HH, Elia N, Ghirlando R, Lippincott-Schwartz J, Hurley JH.

Science. 2008 Oct 24;322(5901):576-80. doi: 10.1126/science.1162042.

11.

Divergent Bro1 domains share the capacity to bind human immunodeficiency virus type 1 nucleocapsid and to enhance virus-like particle production.

Popov S, Popova E, Inoue M, Göttlinger HG.

J Virol. 2009 Jul;83(14):7185-93. doi: 10.1128/JVI.00198-09. Epub 2009 Apr 29.

12.

Viral infection controlled by a calcium-dependent lipid-binding module in ALIX.

Bissig C, Lenoir M, Velluz MC, Kufareva I, Abagyan R, Overduin M, Gruenberg J.

Dev Cell. 2013 May 28;25(4):364-73. doi: 10.1016/j.devcel.2013.04.003. Epub 2013 May 9.

13.

Alix serves as an adaptor that allows human parainfluenza virus type 1 to interact with the host cell ESCRT system.

Boonyaratanakornkit J, Schomacker H, Collins P, Schmidt A.

PLoS One. 2013;8(3):e59462. doi: 10.1371/journal.pone.0059462. Epub 2013 Mar 19.

14.

Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT-independent manner.

Bardens A, Döring T, Stieler J, Prange R.

Cell Microbiol. 2011 Apr;13(4):602-19. doi: 10.1111/j.1462-5822.2010.01557.x. Epub 2010 Dec 28.

PMID:
21129143
15.

CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms.

Katoh K, Shibata H, Hatta K, Maki M.

Arch Biochem Biophys. 2004 Jan 1;421(1):159-65.

PMID:
14678797
16.

The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting.

Katoh K, Shibata H, Suzuki H, Nara A, Ishidoh K, Kominami E, Yoshimori T, Maki M.

J Biol Chem. 2003 Oct 3;278(40):39104-13. Epub 2003 Jul 14.

17.

Super-resolution imaging of ESCRT-proteins at HIV-1 assembly sites.

Prescher J, Baumgärtel V, Ivanchenko S, Torrano AA, Bräuchle C, Müller B, Lamb DC.

PLoS Pathog. 2015 Feb 24;11(2):e1004677. doi: 10.1371/journal.ppat.1004677. eCollection 2015 Feb.

18.

The multiple personalities of Alix.

Odorizzi G.

J Cell Sci. 2006 Aug 1;119(Pt 15):3025-32.

19.

The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release.

Sette P, Mu R, Dussupt V, Jiang J, Snyder G, Smith P, Xiao TS, Bouamr F.

Structure. 2011 Oct 12;19(10):1485-95. doi: 10.1016/j.str.2011.07.016. Epub 2011 Sep 1.

20.

Structural basis for viral late-domain binding to Alix.

Lee S, Joshi A, Nagashima K, Freed EO, Hurley JH.

Nat Struct Mol Biol. 2007 Mar;14(3):194-9. Epub 2007 Feb 4.

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