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Journal Abstract Search

301 related items for PubMed ID: 8836150

  • 1. Prenylation of a Rab1B mutant with altered GTPase activity is impaired in cell-free systems but not in intact mammalian cells.
    Wilson AL, Sheridan KM, Erdman RA, Maltese WA.
    Biochem J; 1996 Sep 15; 318 ( Pt 3)(Pt 3):1007-14. PubMed ID: 8836150
    [Abstract] [Full Text] [Related]

  • 2. The putative "switch 2" domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein.
    Overmeyer JH, Wilson AL, Erdman RA, Maltese WA.
    Mol Biol Cell; 1998 Jan 15; 9(1):223-35. PubMed ID: 9437002
    [Abstract] [Full Text] [Related]

  • 3. Nucleotide dependence of Rab geranylgeranylation. Rab escort protein interacts preferentially with GDP-bound Rab.
    Seabra MC.
    J Biol Chem; 1996 Jun 14; 271(24):14398-404. PubMed ID: 8662963
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  • 4. Association of Rab1B with GDP-dissociation inhibitor (GDI) is required for recycling but not initial membrane targeting of the Rab protein.
    Wilson AL, Erdman RA, Maltese WA.
    J Biol Chem; 1996 May 03; 271(18):10932-40. PubMed ID: 8631911
    [Abstract] [Full Text] [Related]

  • 5. GTP hydrolysis is not important for Ypt1 GTPase function in vesicular transport.
    Richardson CJ, Jones S, Litt RJ, Segev N.
    Mol Cell Biol; 1998 Feb 03; 18(2):827-38. PubMed ID: 9447979
    [Abstract] [Full Text] [Related]

  • 6. Isoprenylation of Rab1B is impaired by mutations in its effector domain.
    Wilson AL, Maltese WA.
    J Biol Chem; 1993 Jul 15; 268(20):14561-4. PubMed ID: 8325834
    [Abstract] [Full Text] [Related]

  • 7. Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI.
    Dirac-Svejstrup AB, Sumizawa T, Pfeffer SR.
    EMBO J; 1997 Feb 03; 16(3):465-72. PubMed ID: 9034329
    [Abstract] [Full Text] [Related]

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  • 9. Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 expressed in cultured cells.
    Erdman RA, Shellenberger KE, Overmeyer JH, Maltese WA.
    J Biol Chem; 2000 Feb 11; 275(6):3848-56. PubMed ID: 10660536
    [Abstract] [Full Text] [Related]

  • 10. Prenylation of Rab5 is dependent on guanine nucleotide binding.
    Sanford JC, Pan Y, Wessling-Resnick M.
    J Biol Chem; 1993 Nov 15; 268(32):23773-6. PubMed ID: 8226909
    [Abstract] [Full Text] [Related]

  • 11. Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases.
    Wilson AL, Erdman RA, Castellano F, Maltese WA.
    Biochem J; 1998 Aug 01; 333 ( Pt 3)(Pt 3):497-504. PubMed ID: 9677305
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  • 14. Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1.
    Vitale N, Moss J, Vaughan M.
    J Biol Chem; 1997 Oct 03; 272(40):25077-82. PubMed ID: 9312116
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  • 15. Activities of mutant Sar1 proteins in guanine nucleotide binding, GTP hydrolysis, and cell-free transport from the endoplasmic reticulum to the Golgi apparatus.
    Saito Y, Kimura K, Oka T, Nakano A.
    J Biochem; 1998 Oct 03; 124(4):816-23. PubMed ID: 9756629
    [Abstract] [Full Text] [Related]

  • 16. Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotides.
    Shapiro AD, Pfeffer SR.
    J Biol Chem; 1995 May 12; 270(19):11085-90. PubMed ID: 7744738
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  • 18. Biochemical and functional characterization of a recombinant GTPase, Rab5, and two of its mutants.
    Hoffenberg S, Sanford JC, Liu S, Daniel DS, Tuvin M, Knoll BJ, Wessling-Resnick M, Dickey BF.
    J Biol Chem; 1995 Mar 10; 270(10):5048-56. PubMed ID: 7890612
    [Abstract] [Full Text] [Related]

  • 19. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange.
    Soldati T, Shapiro AD, Svejstrup AB, Pfeffer SR.
    Nature; 1994 May 05; 369(6475):76-8. PubMed ID: 8164745
    [Abstract] [Full Text] [Related]

  • 20. Conditional activation defect of a human Gsalpha mutant.
    Iiri T, Farfel Z, Bourne HR.
    Proc Natl Acad Sci U S A; 1997 May 27; 94(11):5656-61. PubMed ID: 9159128
    [Abstract] [Full Text] [Related]

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