Vaibhav Bhandari
University of Toronto
8 Papers
9 Citations
Vaibhav Bhandari is an academic researcher from University of Toronto. The author has contributed to research in topics: Biology & Chaperone (protein). The author has an hindex of 5, co-authored 8 publications.
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Papers
The Role of ClpP Protease in Bacterial Pathogenesis and Human Diseases.
TL;DR: The biochemical and cellular activities of ClpP are discussed along with the mechanisms by whichClpP affects bacterial pathogenesis and various human diseases.
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Substrates and interactors of the ClpP protease in the mitochondria.
TL;DR: The ClpP protease is found across eukaryotic and prokaryotic organisms and is well-characterized in bacteria where its function is important in maintaining protein homeostasis as discussed by the authors.
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ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores.
Mark F. Mabanglo,Elisa Leung,Siavash Vahidi,Thiago V. Seraphim,Thiago V. Seraphim,Bryan T. Eger,Steve Bryson,Steve Bryson,Vaibhav Bhandari,Jin Lin Zhou,Yu-Qian Mao,Kamran Rizzolo,Marim M Barghash,Jordan D. Goodreid,Sadhna Phanse,Sadhna Phanse,Mohan Babu,Leandro R.S. Barbosa,Carlos H.I. Ramos,Robert A. Batey,Lewis E. Kay,Emil F. Pai,Walid A. Houry +22 more
- 13 Nov 2019
TL;DR: The structural changes to ClpP from Neisseria meningitidis and Escherichia coli upon binding to two novel activators are examined, showing that reorganization of the electrostatic interaction networks at the ClPP entrance pores is needed for activation.
Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone
S.W.S. Chan,Jason Yau,Christopher Ing,Kaiyin Liu,Patrick Farber,Amy Won,Vaibhav Bhandari,Nareg Kara-Yacoubian,Thiago V. Seraphim,Nilmadhab Chakrabarti,Lewis E. Kay,Christopher M. Yip,Régis Pomès,Simon Sharpe,Walid A. Houry +14 more
TL;DR: It is discovered that a bacterial Escherichia coli chaperone-like ATPase, regulatory ATPase variant A (RavA), and specifically the LARA domain in RavA, forms amyloids under acidic conditions at elevated temperatures.
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Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes.
Alexander Mikaberidze,Thiago V. Seraphim,Thiago V. Seraphim,Nardin Nano,Yiu Wing Sunny Cheung,Siripat Aluksanasuwan,Siripat Aluksanasuwan,Carolina Colleti,Carolina Colleti,Yu-Qian Mao,Vaibhav Bhandari,Gavin Young,Larissa Höll,Sadhna Phanse,Sadhna Phanse,Yuliya Gordiyenko,Daniel R. Southworth,Carol V. Robinson,Visith Thongboonkerd,Lisandra M. Gava,Júlio César Borges,Mohan Babu,Leandro R.S. Barbosa,Carlos H.I. Ramos,Philipp Kukura,Walid A. Houry +25 more
TL;DR: In this article, the principles of R2TP assembly are established and three distinct RUVBL1/2-based complexes are identified: R 2TP, RUV BL1/1-RPAP3 (R2T), and R UVBL 1/2 -PIH 1D1 (R 2P).
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