Crossref journal-article
Springer Science and Business Media LLC
Nature (297)
Bibliography

Daumke, O., Weyand, M., Chakrabarti, P. P., Vetter, I. R., & Wittinghofer, A. (2004). The GTPase-activating protein Rap1GAP uses a catalytic asparagine. Nature, 429(6988), 197–201.

Authors 5
  1. Oliver Daumke (first)
  2. Michael Weyand (additional)
  3. Partha P. Chakrabarti (additional)
  4. Ingrid R. Vetter (additional)
  5. Alfred Wittinghofer (additional)
References 30 Referenced 124
  1. Bos, J. L., de Rooij, J. & Reedquist, K. A. Rap1 signalling: adhering to new models. Nature Rev. Mol. Cell. Biol. 2, 369–377 (2001) (10.1038/35073073) / Nature Rev. Mol. Cell. Biol. by JL Bos (2001)
  2. Hattori, M. & Minato, N. Rap1 GTPase: functions, regulation, and malignancy. J. Biochem. (Tokyo) 134, 479–484 (2003) (10.1093/jb/mvg180) / J. Biochem. (Tokyo) by M Hattori (2003)
  3. Vetter, I. R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299–1304 (2001) (10.1126/science.1062023) / Science by IR Vetter (2001)
  4. Brinkmann, T. et al. Rap-specific GTPase activating protein follows an alternative mechanism. J Biol. Chem. 277, 12525–12531 (2002) (10.1074/jbc.M109176200) / J Biol. Chem. by T Brinkmann (2002)
  5. Rubinfeld, B. et al. Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1. Cell 65, 1033–1042 (1991) (10.1016/0092-8674(91)90555-D) / Cell by B Rubinfeld (1991)
  6. Rubinfeld, B. et al. Localisation of the rap1GAP catalytic domain and sites of phosphorylation by mutational analysis. Mol. Cell. Biol. 12, 4634–4642 (1992) (10.1128/MCB.12.10.4634) / Mol. Cell. Biol. by B Rubinfeld (1992)
  7. Hattori, M. et al. Molecular cloning of a novel mitogen-inducible nuclear protein with a Ran GTPase-activating domain that affects cell cycle progression. Mol Cell. Biol. 15, 552–560 (1995) (10.1128/MCB.15.1.552) / Mol Cell. Biol. by M Hattori (1995)
  8. Gao, Q., Srinivasan, S., Boyer, S. N., Wazer, D. E. & Band, V. The E6 oncoproteins of high-risk papillomaviruses bind to a novel putative GAP protein, E6TP1, and target it for degradation. Mol. Cell. Biol. 19, 733–744 (1999) (10.1128/MCB.19.1.733) / Mol. Cell. Biol. by Q Gao (1999)
  9. Manning, B. D. & Cantley, L. C. Rheb fills a GAP between TSC and TOR. Trends Biochem. Sci. 28, 573–576 (2003) (10.1016/j.tibs.2003.09.003) / Trends Biochem. Sci. by BD Manning (2003)
  10. Gao, Q. et al. Human papillomavirus type 16 E6-induced degradation of E6TP1 correlates with its ability to immortalise human mammary epithelial cells. J. Virol. 75, 4459–4466 (2001) (10.1128/JVI.75.9.4459-4466.2001) / J. Virol. by Q Gao (2001)
  11. Ishida, D. et al. Myeloproliferative stem cell disorders by deregulated Rap1 activation in SPA-1-deficient mice. Cancer Cell 4, 55–65 (2003) (10.1016/S1535-6108(03)00163-6) / Cancer Cell by D Ishida (2003)
  12. Kraemer, A., Brinkmann, T., Plettner, I., Goody, R. & Wittinghofer, A. Fluorescently labelled guanine nucleotide binding proteins to analyse elementary steps of GAP-catalysed reactions. J. Mol. Biol. 324, 763–774 (2002) (10.1016/S0022-2836(02)01136-1) / J. Mol. Biol. by A Kraemer (2002)
  13. Chabre, M. Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology. Trends Biochem. Sci. 15, 6–10 (1990) (10.1016/0968-0004(90)90117-T) / Trends Biochem. Sci. by M Chabre (1990)
  14. Scheffzek, K., Ahmadian, M. R. & Wittinghofer, A. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23, 257–262 (1998) (10.1016/S0968-0004(98)01224-9) / Trends Biochem. Sci. by K Scheffzek (1998)
  15. Maheshwar, M. M. et al. The GAP-related domain of tuberin, the product of the TSC2 gene, is a target for missense mutations in tuberous sclerosis. Hum. Mol. Genet. 6, 1991–1996 (1997) (10.1093/hmg/6.11.1991) / Hum. Mol. Genet. by MM Maheshwar (1997)
  16. Jones, A. C. et al. Comprehensive mutation analysis of TSC1 and TSC2 and phenotypic correlations in 150 families with tuberous sclerosis. Am. J. Hum. Genet. 64, 1305–1315 (1999) (10.1086/302381) / Am. J. Hum. Genet. by AC Jones (1999)
  17. Au, K. S. et al. Germ-line mutational analysis of the TSC2 gene in 90 tuberous-sclerosis patients. Am. J. Hum. Genet. 62, 286–294 (1998) (10.1086/301705) / Am. J. Hum. Genet. by KS Au (1998)
  18. Klose, A. et al. Selective disactivation of neurofibromin GAP activity in neurofibromatosis type 1. Hum. Mol. Genet. 7, 1261–1268 (1998) (10.1093/hmg/7.8.1261) / Hum. Mol. Genet. by A Klose (1998)
  19. Xu, X., Wang, Y., Barry, D. C., Chanock, S. J. & Bokoch, G. M. Guanine nucleotide binding properties of Rac2 mutant proteins and analysis of the responsiveness to guanine nucleotide dissociation stimulator. Biochemistry 36, 626–632 (1997) (10.1021/bi962059h) / Biochemistry by X Xu (1997)
  20. Seewald, M. J., Körner, C., Wittinghofer, A. & Vetter, I. R. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 415, 662–666 (2002) (10.1038/415662a) / Nature by MJ Seewald (2002)
  21. De Antoni, A., Schmitzova, J., Trepte, H. H., Gallwitz, D. & Albert, S. Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs. J. Biol. Chem. 277, 41023–41031 (2002) (10.1074/jbc.M205783200) / J. Biol. Chem. by A De Antoni (2002)
  22. Ahmadian, M. R., Stege, P., Scheffzek, K. & Wittinghofer, A. Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nature Struct. Biol. 4, 686–689 (1997) (10.1038/nsb0997-686) / Nature Struct. Biol. by MR Ahmadian (1997)
  23. Albert, S., Will, E. & Gallwitz, D. Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases. EMBO J. 18, 5216–5225 (1999) (10.1093/emboj/18.19.5216) / EMBO J. by S Albert (1999)
  24. Nassar, N., Hoffman, G. R., Manor, D., Clardy, J. C. & Cerione, R. A. Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nature Struct. Biol. 5, 1047–1052 (1998) (10.1038/4156) / Nature Struct. Biol. by N Nassar (1998)
  25. Graham, D. L., Eccleston, J. F., Chung, C. W. & Lowe, P. N. Magnesium fluoride-dependent binding of small G proteins to their GTPase-activating proteins. Biochemistry 38, 14981–14987 (1999) (10.1021/bi991358e) / Biochemistry by DL Graham (1999)
  26. Goldberg, J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96, 893–902 (1999) (10.1016/S0092-8674(00)80598-X) / Cell by J Goldberg (1999)
  27. Scheffzek, K. et al. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333–338 (1997) (10.1126/science.277.5324.333) / Science by K Scheffzek (1997)
  28. Rittinger, K., Walker, P. A., Eccleston, J. F., Smerdon, S. J. & Gamblin, S. J. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758–762 (1997) (10.1038/39651) / Nature by K Rittinger (1997)
  29. Daumke, O., Wittinghofer, A. & Weyand, M. Purification, crystallisation and preliminary structural characterisation of human Rap1GAP. Acta Crystallogr. D 60, 752–754 (2004) (10.1107/S0907444904002392) / Acta Crystallogr. D by O Daumke (2004)
  30. Lenzen, C., Cool, R. H. & Wittinghofer, A. Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements. Methods Enzymol. 255, 95–109 (1995) (10.1016/S0076-6879(95)55012-7) / Methods Enzymol. by C Lenzen (1995)
Dates
Type When
Created 21 years, 3 months ago (May 12, 2004, 1:33 p.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 2:22 p.m.)
Indexed 3 weeks, 3 days ago (July 28, 2025, 2:18 a.m.)
Issued 21 years, 3 months ago (May 1, 2004)
Published 21 years, 3 months ago (May 1, 2004)
Published Print 21 years, 3 months ago (May 1, 2004)
Funders 0

None

@article{Daumke_2004, title={The GTPase-activating protein Rap1GAP uses a catalytic asparagine}, volume={429}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature02505}, DOI={10.1038/nature02505}, number={6988}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Daumke, Oliver and Weyand, Michael and Chakrabarti, Partha P. and Vetter, Ingrid R. and Wittinghofer, Alfred}, year={2004}, month=may, pages={197–201} }