Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action

Autor: Eckhard Mandelkow, Markus Zweckstetter, Afonso M.S. Duarte, Tatiana Didenko, Tania Morán Luengo, Stefan G.D. Rüdiger, G. Elif Karagöz, Tobias Madl, Chad A. Dickey, Hans Ippel, Bryce A. Nordhues, Jacek Biernat, Rolf Boelens, Elias Akoury, Martina Radli, Dmitry B. Veprintsev

Publikováno v: Cell
Cell, 156(5), 963-974. Cell Press
Europe PubMed Central
Cell 156(5), 963-974 (2014). doi:10.1016/j.cell.2014.01.037
Cell 156, 963-974 (2014)
Cell, 156(5), 963. Cell Press

Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c71a1240dfd843ee70b399e9af2ba17a
https://doi.org/10.1016/j.cell.2014.01.037

Structure and localization of an essential transmembrane segment of the proton translocation channel of yeast H+-V-ATPase

Autor: Carlo P. M. van Mierlo, Nico A. J. van Nuland, Marcus A. Hemminga, Cor J. A. M. Wolfs, Michael A. Harrison, Afonso M.S. Duarte, John B. C. Findlay

Publikováno v: Biochimica et Biophysica Acta. Biomembranes, 1768(2), 218-227
Biochimica et Biophysica Acta. Biomembranes 1768 (2007) 2

Vacuolar (H+)-ATPase (V-ATPase) is a proton pump present in several compartments of eukaryotic cells to regulate physiological processes. From biochemical studies it is known that the interaction between arginine 735 present in the seventh transmembr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::419c1d6cd9d37ad77c8c4ca92e5faf59
https://doi.org/10.1016/j.bbamem.2006.07.014

Molecular dynamics study of the solvation of an alpha-helical transmembrane peptide by DMSO

Autor: Marcus A. Hemminga, Carlo P. M. van Mierlo, Afonso M.S. Duarte

Publikováno v: The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 112(29), 8664-8671
The Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical 112 (2008) 29

A 10-ns molecular dynamics study of the solvation of a hydrophobic transmembrane helical peptide in dimethyl sulfoxide (DMSO) is presented. The objective is to analyze how this aprotic polar solvent is able to solvate three groups of amino acid resid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ccf550f1e2a27cdef0a4247ae526860
https://research.wur.nl/en/publications/molecular-dynamics-study-of-the-solvation-of-an-alpha-helical-tra

Segment TM7 from the cytoplasmic hemi-channel from Vo-H+-V-ATPase includes a flexible region that has a potential role in proton translocation

Autor: Carlo P. M. van Mierlo, Afonso M.S. Duarte, Edwin R. de Jong, Marcus A. Hemminga, Rainer Wechselberger

Publikováno v: Biochimica et Biophysica Acta. Biomembranes, 1768(9), 2263-2270
Biochimica et Biophysica Acta. Biomembranes 1768 (2007) 9

A 900-MHz NMR study is reported of peptide sMTM7 that mimics the cytoplasmic proton hemi-channel domain of the seventh transmembrane segment (TM7) from subunit a of H(+)-V-ATPase from Saccharomyces cerevisiae. The peptide encompasses the amino acid r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::972c2c8222c165adc1e83128487642c2
https://research.wur.nl/en/publications/segment-tm7-from-the-cytoplasmic-hemi-channel-from-vo-h-v-atpase-

A new look into NuoH from Complex I from E. coli

Autor: Bruno C. Marreiros, Manuela M. Pereira, Ana P. Batista, Afonso M.S. Duarte

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817:S54

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dfdfdc7c45623a0757d0147b36eb2c8
https://doi.org/10.1016/j.bbabio.2012.06.154