Structural and Functional Analysis of the ARF1–ARFGAP Complex Reveals a Role for Coatomer in GTP Hydrolysis
- 1 March 1999
- Vol. 96 (6) , 893-902
- https://doi.org/10.1016/s0092-8674(00)80598-x
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Structural analysis of the GAP-related domain from neurofibromin and its implicationsThe EMBO Journal, 1998
- The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras MutantsScience, 1997
- Protein Sorting by Transport VesiclesScience, 1996
- Differential Interaction of the Ras Family GTP-binding Proteins H-Ras, Rap1A, and R-Ras with the Putative Effector Molecules Raf Kinase and Ral-Guanine Nucleotide Exchange FactorPublished by Elsevier ,1996
- The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogueNature, 1995
- GTPase mechanism of Gproteins from the 1.7-Å crystal structure of transducin α - GDP AIF−4Nature, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles.The Journal of cell biology, 1993
- ADP-Ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding proteinCell, 1991
- 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesiclesNature, 1991