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Literature DB >> 32023437

Membrane-Bound Ras as a Conformational Clock.

Alemayehu A Gorfe¹, Stephen G Sligar².

Abstract

Mesh：

Substances：
ras Proteins

Year: 2020 PMID： 32023437 PMCID： PMC7063474 DOI： 10.1016/j.bpj.2020.01.011

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

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14 in total

1. Revealing conformational substates of lipidated N-Ras protein by pressure modulation.

Authors: Shobhna Kapoor; Gemma Triola; Ingrid R Vetter; Mirko Erlkamp; Herbert Waldmann; Roland Winter
Journal: Proc Natl Acad Sci U S A Date: 2011-12-27 Impact factor: 11.205

2. The higher level of complexity of K-Ras4B activation at the membrane.

Authors: Hyunbum Jang; Avik Banerjee; Tanmay S Chavan; Shaoyong Lu; Jian Zhang; Vadim Gaponenko; Ruth Nussinov
Journal: FASEB J Date: 2015-12-30 Impact factor: 5.191

3. Dynamics of Membrane-Bound G12V-KRAS from Simulations and Single-Molecule FRET in Native Nanodiscs.

Authors: Priyanka Prakash; Douglas Litwin; Hong Liang; Suparna Sarkar-Banerjee; Drew Dolino; Yong Zhou; John F Hancock; Vasanthi Jayaraman; Alemayehu A Gorfe
Journal: Biophys J Date: 2018-12-20 Impact factor: 4.033

4. The Plasma Membrane as a Competitive Inhibitor and Positive Allosteric Modulator of KRas4B Signaling.

Authors: Chris Neale; Angel E García
Journal: Biophys J Date: 2020-01-22 Impact factor: 4.033

5. Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site.

Authors: Mohammad T Mazhab-Jafari; Christopher B Marshall; Matthew J Smith; Geneviève M C Gasmi-Seabrook; Peter B Stathopulos; Fuyuhiko Inagaki; Lewis E Kay; Benjamin G Neel; Mitsuhiko Ikura
Journal: Proc Natl Acad Sci U S A Date: 2015-05-04 Impact factor: 11.205

6. K-Ras G-domain binding with signaling lipid phosphatidylinositol (4,5)-phosphate (PIP2): membrane association, protein orientation, and function.

Authors: Shufen Cao; Stacey Chung; SoonJeung Kim; Zhenlu Li; Danny Manor; Matthias Buck
Journal: J Biol Chem Date: 2019-02-21 Impact factor: 5.157

7. Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer.

Authors: Alemayehu A Gorfe; Michael Hanzal-Bayer; Daniel Abankwa; John F Hancock; J Andrew McCammon
Journal: J Med Chem Date: 2007-01-31 Impact factor: 7.446

Membrane-Bound Ras as a Conformational Clock.

1. Revealing conformational substates of lipidated N-Ras protein by pressure modulation.

2. The higher level of complexity of K-Ras4B activation at the membrane.

3. Dynamics of Membrane-Bound G12V-KRAS from Simulations and Single-Molecule FRET in Native Nanodiscs.

4. The Plasma Membrane as a Competitive Inhibitor and Positive Allosteric Modulator of KRas4B Signaling.

5. Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site.

6. K-Ras G-domain binding with signaling lipid phosphatidylinositol (4,5)-phosphate (PIP2): membrane association, protein orientation, and function.

7. Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer.

8. PIP2 Influences the Conformational Dynamics of Membrane-Bound KRAS4b.

9. Interaction of KRas4b with anionic membranes: A special role for PIP₂.

10. Oncogenic K-Ras Binds to an Anionic Membrane in Two Distinct Orientations: A Molecular Dynamics Analysis.

1. Membrane-bound KRAS approximates an entropic ensemble of configurations.

Review 2. A regulatory role of membrane by direct modulation of the catalytic kinase domain.