932 research outputs found
GroEL Ring Separation and Exchange in the Chaperonin Reaction
No full textRaw data for figures published in Cell 172 (2018):
Title: "GroEL Ring Separation and Exchange in the Chaperonin Reaction"
Authors: Xiao Yan, Qiaoyun Shi, Andreas Bracher, Goran Miličić, Amit K. Singh, F. Ulrich Hartl and Manajit Hayer-Hartl.
DOI: http://doi.org/10.1016/j.cell.2017.12.01
Molecular Cell D-17-00395
No full textFull gels for figures published in Molecular Cell article:
Title: "Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase"
Authors: Javaid Y. Bhat, Goran Miličić, Gabriel Thieulin-Pardo, Andreas Bracher, Andrew Maxwell, Susanne Ciniawsky, Oliver Mueller-Cajar, John R. Engen, F. Ulrich Hartl, Petra Wendler, and Manajit Hayer-Hartl.
DOI: http://dx.doi.org/10.1016/j.molcel.2017.07.00
ASCB Award Essays (F. Ulrich Hartl is the corecipient of the 2017 E. B. Wilson Medal awarded by the American Society for Cell Biology.)
No full textProtein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen's discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid and late 1980s, when the chaperone story began to unfold. As a result, we now know that in vivo, protein folding requires assistance by a complex machinery of molecular chaperones. To ensure efficient folding, members of different chaperone classes receive the nascent protein chain emerging from the ribosome and guide it along an ordered pathway toward the native state. I was fortunate to contribute to these developments early on. In this short essay, I will describe some of the critical steps leading to the current concept of protein folding as a highly organized cellular process
GroEL Ring Separation and Exchange in the Chaperonin Reaction
No full textRaw data for figures published in Cell 172 (2018):
Title: "GroEL Ring Separation and Exchange in the Chaperonin Reaction"
Authors: Xiao Yan, Qiaoyun Shi, Andreas Bracher, Goran Miličić, Amit K. Singh, F. Ulrich Hartl and Manajit Hayer-Hartl.
DOI: http://doi.org/10.1016/j.cell.2017.12.01
der Ludwig-Maximilians-Universität München The Eukaryotic Chaperonin TRiC Domain-Wise Folding of Multi-Domain Proteins
No full textI would like to thank Prof. Dr. F.-Ulrich Hartl for giving me the opportunity to work in his laboratory and for his optimism and his creative input during the entire course of my project. I would like to thank my supervisors Dr. Stephanie Etchells and Dr. Andreas Bracher. Many obstacles have been overcome by their support. Their questions and ideas shaped the project significantly. I would like to thank Dr. Markus Stemp who had started the project and who introduced me into many of the necessary skills and techniques. I would like to thank my colleagues in the lab for creating a unique working atmosphere and for many shared moments that I will never forget. I would like to thank Dr. Birgitta Beatrix and Prof. Dr. Don Lamb for the discussions during the TAC meetings that provided helpful external input. I would like to thank the members of my PhD committee PD Dr. Dr. Konstanze Winklhofer, P
Autophagy preferentially degrades non-fibrillar polyQ aggregates
No full textFunder:
http://dx.doi.org/10.13039/501100000781
European Research CouncilFunder:
http://dx.doi.org/10.13039/100005156
Alexander von Humboldt-StiftungFunder:
http://dx.doi.org/10.13039/100018231
Aligning Science Across Parkinson'sFunder:
http://dx.doi.org/10.13039/501100004189
Max-Planck-GesellschaftFunder:
http://dx.doi.org/10.13039/501100000780
European CommissionFunder:
http://dx.doi.org/10.13039/100020668
European Research Executive AgencyFunder:
http://dx.doi.org/10.13039/100010663
European Research CouncilFunder:
http://dx.doi.org/10.13039/501100001659
Deutsche Forschungsgemeinschaf
Molecular Mechanism of Protein Folding in the Cell
No full textF.-Ulrich Hartl and Arthur Horwich will share this year's Lasker Basic Medical Science Award for the discovery of the cell's protein-folding machinery, exemplified by cage-like structures that convert newly synthesized proteins into their biologically active forms. Their fundamental findings reveal mechanisms that operate in normal physiologic processes and help to explain the problems that arise in diseases of protein folding
Correction to: Gel‐like inclusions of C‐terminal fragments of TDP‐43 sequester stalled proteasomes in neurons (EMBO reports, (2022), 23, 6, (e53890), 10.15252/embr.202153890)
No full text(Figure presented.)</p
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