Pallav Kosuri

Affiliations: 
Harvard University, Cambridge, MA, United States 
Area:
Molecular biophysics
Google:
"Pallav Kosuri"
Mean distance: 15.74 (cluster 11)
 
SNBCP
Cross-listing: Neurotree

Parents

Sign in to add mentor
Julio Fernandez grad student 2012 Columbia
 (Mechanochemical Methods for Single Molecule Biochemistry and Studies of Thiol-Disulfide Exchange in Proteins.)
Xiaowei Zhuang post-doc 2013- Harvard
BETA: Related publications

Publications

You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect.

Lee H, Yu CC, Boyden ES, et al. (2021) Tetra-gel enables superior accuracy in combined super-resolution imaging and expansion microscopy. Scientific Reports. 11: 16944
Kosuri P, Altheimer BD, Dai M, et al. (2019) Rotation tracking of genome-processing enzymes using DNA origami rotors. Nature
Kosuri P, Altheimer B, Dai M, et al. (2018) High-throughput Rotation Tracking using DNA Origami Rotors Biophysical Journal. 114: 389a
Altheimer BD, Kosuri P, Dai M, et al. (2017) High-Resolution Single Molecule Rotation Tracking of RecBCD using DNA Origami Rotors Biophysical Journal. 112: 170a
Rivas-Pardo JA, Eckels EC, Popa I, et al. (2016) Work Done by Titin Protein Folding Assists Muscle Contraction. Cell Reports
Rivas Pardo JA, Eckels EC, Popa I, et al. (2016) Protein Folding Drives Muscle Contraction Biophysical Journal. 110: 636a
Rivas Pardo JA, Eckels EC, Popa I, et al. (2015) Direct Observation of Titin Immunoglobulin Domain Unfolding-Refolding in Muscle Sarcomeres Biophysical Journal. 108: 170a
Alegre-Cebollada J, Kosuri P, Giganti D, et al. (2014) S-glutathionylation of cryptic cysteines enhances titin elasticity by blocking protein folding. Cell. 156: 1235-46
Alegre-Cebollada J, Kosuri P, Giganti D, et al. (2014) Large-Scale Modulation of Titin Elasticity by S-Glutathionylation of Cryptic Cysteines Biophysical Journal. 106: 454a
Popa I, Kosuri P, Alegre-Cebollada J, et al. (2013) Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy. Nature Protocols. 8: 1261-76
See more...