Bharat V Adkar

Scopus Author ID Loop profile ORCID

Publication Activity (10 Years)

Years Active: 2017-2023
Publications (10 Years): 12

Top Topics

Structural Basis

Single Molecule

Tyrosine Kinase

Top Venues

Proceedings of the National Academy of Sciences of the United States of America

Nature ecology & evolution

Molecular systems biology

Proceedings. Biological sciences

This page only lists publications with an associated author ORCID identifier.

Publications

David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
David Scheerer, Bharat V Adkar, Sanchari Bhattacharyya, Dorit Levy, Marija Iljina, Inbal Riven, Orly Dym, Gilad Haran, Eugene I Shakhnovich
Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the United States of America 120 (18) (2023)
Sanchari Bhattacharyya, Shimon Bershtein, Bharat V Adkar, Jaie Woodard, Eugene I Shakhnovich
Metabolic response to point mutations reveals principles of modulation of in vivo enzyme activity and phenotype. Molecular systems biology 17 (6) (2022)
Michael Manhart, Bharat V Adkar, Eugene I Shakhnovich
Trade-offs between microbial growth phases lead to frequency-dependent and non-transitive selection. Proceedings. Biological sciences 285 (1872) (2019)
Bharat V Adkar, Sanchari Bhattacharyya, Amy I Gilson, Wenli Zhang, Eugene I Shakhnovich
Substrate inhibition imposes fitness penalty at high protein stability. Proceedings of the National Academy of Sciences of the United States of America 116 (23) (2019)
Bharat V Adkar, Michael Manhart, Sanchari Bhattacharyya, Jian Tian, Michael Musharbash, Eugene I Shakhnovich
Optimization of lag phase shapes the evolution of a bacterial enzyme. Nature ecology & evolution 1 (6) (2017)