The Guanine Nucleotide-Binding Switch in Three Dimensions

By I. Vetter, A. Wittinghofer. Science, 2001

1,897 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/c2b198e68b263e267d7a0d8e5387b9ec68559cce

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. C. Der
2. Krister Wennerberg
3. K. Shannon
4. G. Bollag
5. Suzanne Schubbert

In Molecular Biology

1. Avner Schlessinger
2. Burkhard Rost
3. Rodrigo Vargas Honorato
4. C. Der
5. Alexandre M. J. J. Bonvin
6. K. Rossman
7. Krister Wennerberg
8. G. Bollag

In Physiology

1. C. Der
2. Krister Wennerberg
3. K. Shannon
4. G. Bollag
5. Suzanne Schubbert
6. Manuel Serrano
7. P. Cossart
8. S. Mostowy

Citations in the corpus

• Targeting the Mitogen-Activated Protein Kinase RAS-RAF Signaling Pathway in Cancer Therapy (2012, background): “G proteins act as molecular switches and timers that cycle from inactive GDP-bound to active GTP-bound states [14].”
• Rho-family GTPases: it's not only Rac and Rho (and I like it) (2004, background): “In common with Ras and other small GTPases, the GDPand GTP-bound states of the classical Rho GTPases differ in conformation primarily in two localized regions, switch I and II, and this feature is probably shared by all Rho GTPases (Vetter and Wittinghofer, 2001).”
• Hyperactive Ras in developmental disorders and cancer (2007, background): “Tiam1 mediates Ras activation of Rac by a PI(3)K-independent mechanism.”
• Germline KRAS mutations cause Noonan syndrome (2006, background): “Ras proteins regulate cell fates by cycling between active guanosine triphosphate (GTP)-bound and inactive guanosine diphosphate (GDP)-bound conformations (Ras-GTP and Ras-GDP) (reviewed in refs”
• Hyperactive Ras in developmental disorders and cancer (2007, background): “Tiam1 mediates Ras activation of Rac by a PI(3)K-independent mechanism.”
• Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development (2020, background): “GTPases, including RAS proteins, have a built-in switch mechanism that allows the protein to adopt an active conformation, capable of binding effector proteins when GTP is bound [97].”
• A comprehensive survey of Ras mutations in cancer (2012, neutral): “Residues that aremutated in cancer are highlighted in red, those that are mutated in developmental disorders are underlined, and those that are variable among isoforms are in gray (26, 65, 66).”
• The Ras superfamily at a glance (2005, background): “Ras superfamily GTPases function as GDP/GTP-regulated molecular switches ( Vetter and Wittinghofer, 2001 ).”
• Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex (2002, background): “Dock180 does not contain the Dbl homology (DH) domain present in all known mammalian Rac guanine nucleotide exchange factors (GEFs”
• Protein flexibility and rigidity predicted from sequence (2005, background): “9-residue segment is Gln61 which is the catalytic residue of the reaction.(71,72) A recent study showed that the”
• eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining (2014, background): “The transition between the two states is defined by conformational changes in two dynamic elements of the G domain, termed switch 1 and switch 2, which specifically interact with the c-phosphate of the GTP molecule (Vetter & Wittinghofer, 2001).”