The structure and oxidation of the eye lens chaperone αA-crystallin

Autor: Philipp W. N. Schmid, Bernd Reif, Beate Rockel, Sam Asami, Juri Rappsilber, Martin Haslbeck, Carsten Peters, Martin Zacharias, Evgeny V. Mymrikov, Juan Zou, Maria Stavropoulou, Christoph J. O. Kaiser, Sevil Weinkauf, Johannes Buchner, Vinay Dahiya

Publikováno v: Kaiser, C J O, Peters, C, Schmid, P W N, Stavropoulou, M, Zou, J, Dahiya, V, Mymrikov, E V, Rockel, B, Asami, S, Haslbeck, M, Rappsilber, J, Reif, B, Zacharias, M, Buchner, J & Weinkauf, S 2019, ' The structure and oxidation of the eye lens chaperone αA-crystallin ', Nature Structural and Molecular Biology, vol. 26, no. 12, pp. 1141-1150 . https://doi.org/10.1038/s41594-019-0332-9
Nat. Struct. Mol. Biol. 26, 1141-1150 (2019)
Nature structural & molecular biology

The small heat shock protein αA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human αA-crystallin oligomers by combi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4a3bc49d8b425998f5e56665a53e3f
https://www.pure.ed.ac.uk/ws/files/131168653/TheStructureAndOxidationOfTheEyesLensChaperone.pdf

The Structure of Human Tripeptidyl Peptidase II as Determined by a Hybrid Approach

Autor: Elizabeth Villa, Friedrich Förster, Beate Rockel, Anne-Marie Schönegge, Reiner Hegerl, Jürgen Peters, Wolfgang Baumeister

Publikováno v: Structure. 20(4):593-603

SummaryTripeptidyl-peptidase II (TPPII) is a high molecular mass (∼5 MDa) serine protease, which is thought to act downstream of the 26S proteasome, cleaving peptides released by the latter. Here, the structure of human TPPII (HsTPPII) has been det

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb355486d85c472d88d788b11d0468a4

Visualizing cells at the nanoscale

Autor: Andrew Leis, Beate Rockel, Lars Andrees, Wolfgang Baumeister

Publikováno v: Trends in Biochemical Sciences. 34:60-70

Cryogenic electron tomography (cryo- ET) enables the 3D visualization of biological material at a previously unseeable scale. Carefully controlled cryogenic specimen preparation avoids the artefacts that are notorious to conventional electron microsc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7250fbab6b1929407bf99cbf4bfe9d06
https://doi.org/10.1016/j.tibs.2008.10.011

Aberration-corrected microscopy for structural biology applications

Autor: Reiner Hegerl, Beate Rockel, Bert Freitag, Jürgen M. Plitzko, A. Ziegler, U. Lucken

Publikováno v: Journal of Microscopy. 233:170-177

This study explores the potential of a C(s)-corrected transmission electron microscope for structural studies of biological samples, in particular isolated macromolecular complexes. A 300-kV transmission electron microscope, equipped with a C(s) corr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f7c01a326f2c797bd0c020d72478309
https://doi.org/10.1111/j.1365-2818.2008.03106.x

VAT, the Thermoplasma Homolog of Mammalian p97/VCP, Is an N Domain-regulated Protein Unfoldase

Autor: Beate Rockel, Tomohiro Tamura, Peter Zwickl, Jürgen Peters, Alexandra Gerega, Wolfgang Baumeister

Publikováno v: Journal of Biological Chemistry. 280:42856-42862

The Thermoplasma VCP-like ATPase from Thermoplasma acidophilum (VAT) ATPase is a member of the two-domain AAA ATPases and homologous to the mammalian p97/VCP and NSF proteins. We show here that the VAT ATPase complex unfolds green fluorescent protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df579dc097958d11207faf33e9a8b825
https://doi.org/10.1074/jbc.m510592200