✦ LIBER ✦

Interaction of G protein Gβγ dimers with small GTP-binding proteins of the Rho family

✍ Scribed by Rainer Harhammer; Antje Gohla; Günter Schultz

Book ID: 117106856
Publisher: Elsevier Science
Year: 1996
Tongue: English
Weight: 398 KB
Volume: 399
Category: Article
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(96)01327-0

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Interaction of radixin with Rho small G

Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl

✍ Takahashi, Kazuo; Sasaki, Takuya; Mammoto, Akiko; Hotta, Ikuko; Takaishi, Kenji; 📂 Article 📅 1998 🏛 Nature Publishing Group 🌐 English ⚖ 354 KB

Interaction of the Rho Family Small G Pr

Interaction of the Rho Family Small G Proteins with Kinectin, an Anchoring Protein of Kinesin Motor

✍ Kazuhiko Hotta; Kazuma Tanaka; Akihisa Mino; Hideshi Kohno; Yoshimi Takai 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 110 KB

Small GTP-Binding Proteins of the Rho Fa

Small GTP-Binding Proteins of the Rho Family in the Dictyostelium Cytoskeleton

✍ Francisco Rivero; Angelika A. Noegel 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 588 KB

Association of the Rho family small GTP-

Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae

✍ Koch, Gertrude; Tanaka, Kazuma; Masuda, Tadayuki; Yamochi, Wataru; Nonaka, Hidet 📂 Article 📅 1997 🏛 Nature Publishing Group 🌐 English ⚖ 423 KB

Interaction of Gβ3s, a splice variant of

Interaction of Gβ3s, a splice variant of the G-protein Gβ3, with Gγ- and Gα-proteins

✍ Dieter Rosskopf; Karin Koch; Christiane Habich; Jörg Geerdes; Axel Ludwig; Sabin 📂 Article 📅 2003 🏛 Elsevier Science 🌐 English ⚖ 403 KB

Conformational flexibility and binding i

Conformational flexibility and binding interactions of the G protein βγ heterodimer

✍ Min-Sun Park; Alan V. Smrcka; Harry A. Stern 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 739 KB

## Abstract Previous NMR experiments on unbound G protein βγ heterodimer suggested that particular residues in the binding interface are mobile on the nanosecond timescale. In this work we performed nanosecond‐timescale molecular dynamics simulations to investigate conformational changes and dynami