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1687 Publications visible to you, out of a total of 1687
Formation of sdB-stars via common envelope ejection by substellar companions

Abstract

Not specified

Authors: M. Kramer, F. R. N. Schneider, S. T. Ohlmann, S. Geier, V. Schaffenroth, R. Pakmor, F. K. Röpke

Date Published: 1st Oct 2020

Publication Type: Journal

New technical approaches for 3D morphological imaging and quantification of measurements

Abstract

Not specified

Authors: Cinzia Brenna, Arif ul Maula Khan, Tiziana Picascia, Quanchao Sun, Vincent Heuveline, Norbert Gretz

Date Published: 1st Oct 2020

Publication Type: Journal

VizieR Online Data Catalog: OB stars TESS phot. & high-resolution spectroscopy (Bowman+, 2020)

Abstract

Not specified

Authors: D. M. Bowman, S. Burssens, S. Simon-Diaz, P. V. F. Edelmann, T. M. Rogers, L. Horst, F. K. Ropke, C. Aerts

Date Published: 1st Oct 2020

Publication Type: Journal

Formation of sdB-stars via common envelope ejection by substellar companions

Abstract

Not specified

Authors: M. Kramer, F. R. N. Schneider, S. T. Ohlmann, S. Geier, V. Schaffenroth, R. Pakmor, F. K. Röpke

Date Published: 1st Oct 2020

Publication Type: Journal

Structural basis of Focal Adhesion Kinase activation on lipid membranes.

Abstract (Expand)

Focal adhesion kinase (FAK) is a key component of the membrane proximal signaling layer in focal adhesion complexes, regulating important cellular processes, including cell migration, proliferation, … and survival. In the cytosol, FAK adopts an autoinhibited state but is activated upon recruitment into focal adhesions, yet how this occurs or what induces structural changes is unknown. Here, we employ cryo-electron microscopy to reveal how FAK associates with lipid membranes and how membrane interactions unlock FAK autoinhibition to promote activation. Intriguingly, initial binding of FAK to the membrane causes steric clashes that release the kinase domain from autoinhibition, allowing it to undergo a large conformational change and interact itself with the membrane in an orientation that places the active site toward the membrane. In this conformation, the autophosphorylation site is exposed and multiple interfaces align to promote FAK oligomerization on the membrane. We show that interfaces responsible for initial dimerization and membrane attachment are essential for FAK autophosphorylation and resulting cellular activity including cancer cell invasion, while stable FAK oligomerization appears to be needed for optimal cancer cell proliferation in an anchorage-independent manner. Together, our data provide structural details of a key membrane bound state of FAK that is primed for efficient autophosphorylation and activation, hence revealing the critical event in integrin mediated FAK activation and signaling at focal adhesions.

Authors: Iván Acebrón, Ricardo D Righetto, Christina Schoenherr, Svenja de Buhr, Pilar Redondo, Jayne Culley, Carlos F Rodríguez, Csaba Daday, Nikhil Biyani, Oscar Llorca, Adam Byron, Mohamed Chami, Frauke Gräter, Jasminka Boskovic, Margaret C Frame, Henning Stahlberg, Daniel Lietha

Date Published: 1st Oct 2020

Publication Type: Journal

A workflow for exploring ligand dissociation from a macromolecule: Efficient random acceleration molecular dynamics simulation and interaction fingerprint analysis of ligand trajectories

Abstract

Not specified

Authors: Daria B. Kokh, Bernd Doser, Stefan Richter, Fabian Ormersbach, Xingyi Cheng, Rebecca C. Wade

Date Published: 28th Sep 2020

Publication Type: Journal

Analysis and Numerical Approximation of Dielectrophoretic Force Driven Flow Problems

Abstract

Not specified

Author: Philipp Gerstner

Date Published: 11th Sep 2020

Publication Type: Doctoral Thesis

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