Author

M. Baruah

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Approach:deep learning· 1 Approach:experimental assay· 1 Assay:proteomics· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

A. K. Shukla· 2 shared A. Ranjan· 2 shared B. Panigrahi· 1 shared D. Devost· 1 shared H. Dwivedi-Agnihotri· 1 shared I. Petrovic· 1 shared J. Maharana· 1 shared J. Selent· 1 shared

Activity by Year

2022-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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2 shared papersBiophysics

A. K. Shukla

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2 papers

Recent·Most cited

A key GPCR phosphorylation motif discovered in arrestin2-CCR5 phosphopeptide complexes

P. Isaikina, I. Petrovic, R. P. Jakob, P. Sarma, A. Ranjan, M. Baruah, V. Panwalkar, T. Maier, A. K. Shukla, S. Grzesiek

The paper identifies a phosphorylation motif in arrestin2-CCR5 complexes that is essential for stable interactions and functional activation of CCR5.

bioRxiv · Oct 10, 2022 · PreprintBiophysics

Allosteric modulation of GPCR-induced β-arrestin trafficking and signaling by a synthetic intrabody

M. Baidya, M. Chaturvedi, H. Dwivedi-Agnihotri, A. Ranjan, D. Devost, Y. Namkung, T. M. Stepniewski, S. Pandey, M. Baruah, B. Panigrahi, J. Maharana, R. Banerjee, J. Selent, S. Laporte, T. E. Hebert, A. K. Shukla

This paper shows that a synthetic intrabody enhances β-arrestin endosomal trafficking and ERK1/2 activation in a GPCR mutant by promoting an active-like conformation.

bioRxiv · Jan 11, 2022Biochemistry