G
Georg K. A. Hochberg
Researcher at Max Planck Society
Publications - 41
Citations - 1678
Georg K. A. Hochberg is an academic researcher from Max Planck Society. The author has contributed to research in topics: Biology & Medicine. The author has an hindex of 12, co-authored 24 publications receiving 1154 citations. Previous affiliations of Georg K. A. Hochberg include University of Marburg & University of Oxford.
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Journal ArticleDOI
Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles.
Michael T. Marty,Andrew Baldwin,Erik G. Marklund,Georg K. A. Hochberg,Justin L. P. Benesch,Carol V. Robinson +5 more
TL;DR: UniDec (Universal Deconvolution), software that provides a rapid, robust, and flexible deconvolution of mass spectra and ion mobility-mass spectra with minimal user intervention is developed, using systems of increasing complexity.
Journal ArticleDOI
The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity
Georg K. A. Hochberg,Heath Ecroyd,Heath Ecroyd,Cong Liu,Cong Liu,Cong Liu,Dezerae Cox,Dezerae Cox,Duilio Cascio,Duilio Cascio,Duilio Cascio,Michael R. Sawaya,Michael R. Sawaya,Michael R. Sawaya,Miranda P. Collier,James C. Stroud,James C. Stroud,James C. Stroud,John A. Carver,Andrew Baldwin,Carol V. Robinson,David Eisenberg,David Eisenberg,Justin L. P. Benesch,Arthur Laganowsky +24 more
TL;DR: It is found that the core domain of the human molecular chaperone αB-crystallin can function effectively in preventing protein aggregation and amyloid toxicity, and is designed as an equivalently locked cABC to investigate the functional role played by oligomerization, disordered N and C termini, subunit exchange, and variable dimer interfaces in ABC.
The s tructured core domain of αB-crystallin can prevent amyloid fi brillation and associated toxicity
TL;DR: In this article, the core domain of the human molecular chaperone αB-crystallin can function effectively in preventing protein aggregation and amyloid toxicity, and the structures of these domains that are presented should represent useful scaffolds for the design of novel AMyloid inhibitors.
Journal ArticleDOI
Reconstructing Ancient Proteins to Understand the Causes of Structure and Function.
TL;DR: Recent studies employing ancestral protein reconstruction are reviewed and it is shown how they have produced new knowledge not only of molecular evolutionary processes but also of the underlying determinants of modern proteins' physical, chemical, and biological properties.
Journal ArticleDOI
An ultra-stable gold-coordinated protein cage displaying reversible assembly.
Ali D. Malay,Naoyuki Miyazaki,Artur Biela,Soumyananda Chakraborti,Karolina Majsterkiewicz,Izabela Stupka,Craig S. Kaplan,Agnieszka Kowalczyk,Bernard Piette,Georg K. A. Hochberg,Georg K. A. Hochberg,Di Wu,Tomasz P. Wrobel,Adam Fineberg,Manish S. Kushwah,Mitja Kelemen,Primož Vavpetič,Primož Pelicon,Philipp Kukura,Justin L. P. Benesch,Kenji Iwasaki,Kenji Iwasaki,Jonathan G. Heddle +22 more
TL;DR: This work establishes an approach for linking protein components into robust, higher-order structures, and expands the design space available for supramolecular assemblies to include previously unexplored geometries, and displays excellent chemical and thermal stability.