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Journal Abstract Search

268 related items for PubMed ID: 19143621

  • 1. Evolution and assembly of ESCRTs.
    Ghazi-Tabatabai S, Obita T, Pobbati AV, Perisic O, Samson RY, Bell SD, Williams RL.
    Biochem Soc Trans; 2009 Feb; 37(Pt 1):151-5. PubMed ID: 19143621
    [Abstract] [Full Text] [Related]

  • 2. Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4.
    Obita T, Saksena S, Ghazi-Tabatabai S, Gill DJ, Perisic O, Emr SD, Williams RL.
    Nature; 2007 Oct 11; 449(7163):735-9. PubMed ID: 17928861
    [Abstract] [Full Text] [Related]

  • 3. Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs).
    Han H, Monroe N, Votteler J, Shakya B, Sundquist WI, Hill CP.
    J Biol Chem; 2015 May 22; 290(21):13490-9. PubMed ID: 25833946
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  • 4. Structural Fine-Tuning of MIT-Interacting Motif 2 (MIM2) and Allosteric Regulation of ESCRT-III by Vps4 in Yeast.
    Kojima R, Obita T, Onoue K, Mizuguchi M.
    J Mol Biol; 2016 Jun 05; 428(11):2392-2404. PubMed ID: 27075672
    [Abstract] [Full Text] [Related]

  • 5. Membrane scission by the ESCRT-III complex.
    Wollert T, Wunder C, Lippincott-Schwartz J, Hurley JH.
    Nature; 2009 Mar 12; 458(7235):172-7. PubMed ID: 19234443
    [Abstract] [Full Text] [Related]

  • 6. Conformational Changes in the Endosomal Sorting Complex Required for the Transport III Subunit Ist1 Lead to Distinct Modes of ATPase Vps4 Regulation.
    Tan J, Davies BA, Payne JA, Benson LM, Katzmann DJ.
    J Biol Chem; 2015 Dec 11; 290(50):30053-65. PubMed ID: 26515066
    [Abstract] [Full Text] [Related]

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  • 8. The linker region plays a regulatory role in assembly and activity of the Vps4 AAA ATPase.
    Shestakova A, Curtiss M, Davies BA, Katzmann DJ, Babst M.
    J Biol Chem; 2013 Sep 13; 288(37):26810-9. PubMed ID: 23913684
    [Abstract] [Full Text] [Related]

  • 9. Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation.
    Adell MA, Vogel GF, Pakdel M, Müller M, Lindner H, Hess MW, Teis D.
    J Cell Biol; 2014 Apr 14; 205(1):33-49. PubMed ID: 24711499
    [Abstract] [Full Text] [Related]

  • 10. Coevolution of Eukaryote-like Vps4 and ESCRT-III Subunits in the Asgard Archaea.
    Lu Z, Fu T, Li T, Liu Y, Zhang S, Li J, Dai J, Koonin EV, Li G, Chu H, Li M.
    mBio; 2020 May 19; 11(3):. PubMed ID: 32430468
    [Abstract] [Full Text] [Related]

  • 11. ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1.
    Azmi IF, Davies BA, Xiao J, Babst M, Xu Z, Katzmann DJ.
    Dev Cell; 2008 Jan 19; 14(1):50-61. PubMed ID: 18194652
    [Abstract] [Full Text] [Related]

  • 12. Vps4 regulates a subset of protein interactions at the multivesicular endosome.
    Vajjhala PR, Catchpoole E, Nguyen CH, Kistler C, Munn AL.
    FEBS J; 2007 Apr 19; 274(8):1894-907. PubMed ID: 17408385
    [Abstract] [Full Text] [Related]

  • 13. Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation.
    Teis D, Saksena S, Emr SD.
    Dev Cell; 2008 Oct 19; 15(4):578-89. PubMed ID: 18854142
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  • 15. Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes.
    Nickerson DP, West M, Odorizzi G.
    J Cell Biol; 2006 Dec 04; 175(5):715-20. PubMed ID: 17130288
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  • 17. Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4.
    Xiao J, Xia H, Yoshino-Koh K, Zhou J, Xu Z.
    J Mol Biol; 2007 Nov 30; 374(3):655-70. PubMed ID: 17949747
    [Abstract] [Full Text] [Related]

  • 18. Assembly of the AAA ATPase Vps4 on ESCRT-III.
    Shestakova A, Hanono A, Drosner S, Curtiss M, Davies BA, Katzmann DJ, Babst M.
    Mol Biol Cell; 2010 Mar 15; 21(6):1059-71. PubMed ID: 20110351
    [Abstract] [Full Text] [Related]

  • 19. ESCRT-III recognition by VPS4 ATPases.
    Stuchell-Brereton MD, Skalicky JJ, Kieffer C, Karren MA, Ghaffarian S, Sundquist WI.
    Nature; 2007 Oct 11; 449(7163):740-4. PubMed ID: 17928862
    [Abstract] [Full Text] [Related]

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