Arun P. Wiita, Ph.D.

Columbia University, New York, NY 
"Arun Wiita"
Mean distance: 15.74 (cluster 11)


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Julio Fernandez grad student 2008 Columbia
 (Probing chemistry and catalysis in single protein molecules with mechanical force.)
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Huang HH, Ferguson ID, Thornton AM, et al. (2020) Proteasome inhibitor-induced modulation reveals the spliceosome as a specific therapeutic vulnerability in multiple myeloma. Nature Communications. 11: 1931
Choudhry P, Galligan D, Wiita AP. (2018) Seeking Convergence and Cure with New Myeloma Therapies. Trends in Cancer. 4: 567-582
Ferguson I, Lam C, Mariano MC, et al. (2018) Novel Allosteric Inhibitors of Heat Shock Protein 70 As Agents to Probe Protein Homeostasis and Overcome Proteasome Inhibitor Resistance in Multiple Myeloma Blood. 132: 3212-3212
Le Moigne R, Aftab BT, Djakovic S, et al. (2017) The p97 inhibitor CB-5083 is a unique disrupter of protein homeostasis in models of Multiple Myeloma. Molecular Cancer Therapeutics
Liu TY, Huang HH, Wheeler D, et al. (2017) Time-Resolved Proteomics Extends Ribosome Profiling-Based Measurements of Protein Synthesis Dynamics. Cell Systems
Julien O, Zhuang M, Wiita AP, et al. (2016) Quantitative MS-based enzymology of caspases reveals distinct protein substrate specificities, hierarchies, and cellular roles. Proceedings of the National Academy of Sciences of the United States of America
Wiita AP, Seaman JE, Wells JA. (2014) Global analysis of cellular proteolysis by selective enzymatic labeling of protein N-termini. Methods in Enzymology. 544: 327-58
Perez-Jimenez R, Li J, Kosuri P, et al. (2009) Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy. Nature Structural & Molecular Biology. 16: 890-6
Perez-Jimenez R, Wiita AP, Rodriguez-Larrea D, et al. (2008) Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis. The Journal of Biological Chemistry. 283: 27121-9
Koti Ainavarapu SR, Wiita AP, Dougan L, et al. (2008) Single-molecule force spectroscopy measurements of bond elongation during a bimolecular reaction. Journal of the American Chemical Society. 130: 6479-87
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