M
Manish S. Kushwah
Researcher at University of Oxford
Publications - 10
Citations - 194
Manish S. Kushwah is an academic researcher from University of Oxford. The author has contributed to research in topics: Lipid bilayer & Chemistry. The author has an hindex of 2, co-authored 8 publications receiving 77 citations.
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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.
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Mass photometry enables label-free tracking and mass measurement of single proteins on lipid bilayers.
TL;DR: In this article, the authors demonstrate dynamic mass photometry, a method for label-free imaging, tracking and mass measurement of individual membrane-associated proteins diffusing on supported lipid bilayers.
Journal ArticleDOI
The linear ubiquitin chain assembly complex (LUBAC) generates heterotypic ubiquitin chains.
Alan Rodriguez Carvajal,Irina Grishkovskaya,Carlos Gomez Diaz,Antonia Vogel,Adar Sonn-Segev,Manish S. Kushwah,Katrin Schodl,Luiza Deszcz,Luiza Deszcz,Zsuzsanna Orban-Nemeth,Shinji Sakamoto,Karl Mechtler,Philipp Kukura,Tim Clausen,David Haselbach,Fumiyo Ikeda,Fumiyo Ikeda +16 more
TL;DR: In this paper, a 3D reconstruction of human linear ubiquitin chain assembly complex (LUBAC) was obtained by electron microscopy and reported its generation of heterotypic chains containing linear linkages with oxyester-linked branches.
Journal ArticleDOI
Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
TL;DR: In this article, a single molecule mass photometry quantifies affinity and polydispersity of heterogeneous protein complexes in solution, and the authors demonstrate these capabilities by studying the functionally relevant 2-cysteine peroxiredoxins (2CPs).
Posted ContentDOI
Single Molecule Mass Photometry Reveals Dynamic Oligomerization of Plant and Human Peroxiredoxins for Functional Conservation and Diversification
TL;DR: In this paper, single molecule mass photometry was used to study the dynamic equilibria of the ubiquitous and highly abundant 2-Cysteine peroxiredoxins (2-CysPRX).