User profiles for Nikhil P. Damle
Nikhil DamleOsthus GmbH Verified email at bioss.uni-freiburg.de Cited by 235 |
[PDF][PDF] Systematic discovery of short linear motifs decodes calcineurin phosphatase signaling
CP Wigington, J Roy, NP Damle, VK Yadav, C Blikstad… - Molecular cell, 2020 - cell.com
Short linear motifs (SLiMs) drive dynamic protein-protein interactions essential for signaling,
but sequence degeneracy and low binding affinities make them difficult to identify. We …
but sequence degeneracy and low binding affinities make them difficult to identify. We …
The human DEPhOsphorylation database DEPOD: 2019 update
… Nikhil P Damle , Nikhil P Damle … Nikhil P Damle, Maja Köhn, The human DEPhOsphorylation
Database DEPOD: 2019 update, Database, Volume 2019, 2019, baz133, https://doi.org/…
Database DEPOD: 2019 update, Database, Volume 2019, 2019, baz133, https://doi.org/…
Quantitative mapping of protein-peptide affinity landscapes using spectrally encoded beads
10.7554/eLife.40499.001 Transient, regulated binding of globular protein domains to Short
Linear Motifs (SLiMs) in disordered regions of other proteins drives cellular signaling. …
Linear Motifs (SLiMs) in disordered regions of other proteins drives cellular signaling. …
[HTML][HTML] LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation
The Mycobacterium tuberculosis kinase PknB is essential for growth and survival of the
pathogen in vitro and in vivo. Here we report the results of our efforts to elucidate the mechanism …
pathogen in vitro and in vivo. Here we report the results of our efforts to elucidate the mechanism …
Experimental and analytical study of the hydrodynamic and single and two-phase convective heat transfer performance of flexible PDMS microchannels with …
N Damle, Y Joshi - Applied Thermal Engineering, 2023 - Elsevier
Various copper and silicon based thermal management systems are used in the cooling of
electronics. However, the rigid nature of these materials along with their high thermal and …
electronics. However, the rigid nature of these materials along with their high thermal and …
Mechanism of autophosphorylation of mycobacterial PknB explored by molecular dynamics simulations
Mycobacterial Ser/Thr kinase, PknB, is essential for the growth of the pathogen. Unphosphorylated
PknB is catalytically inactive, and its activation requires autophosphorylation of Thr …
PknB is catalytically inactive, and its activation requires autophosphorylation of Thr …
[PDF][PDF] SW3 6JB, UK
CP Wigington1&, J Roy1&, NP Damle, VK Yadav… - scholar.archive.org
Short linear motifs (SLiMs) drive dynamic protein-protein interactions essential for signaling,
but sequence degeneracy and low binding affinities make them difficult to identify. We …
but sequence degeneracy and low binding affinities make them difficult to identify. We …
Uncovering Novel Substrates and Functions for the Calcineurin Phosphatase in Human Cells
CP Wigington, J Roy, NP Damle, SE Cho… - The FASEB …, 2017 - Wiley Online Library
Protein phosphatases play essential roles in every signaling pathway; however, systems‐level
understanding of phosphatase signaling networks is lacking due to the inherent …
understanding of phosphatase signaling networks is lacking due to the inherent …
LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation
The Mycobacterium tuberculosis kinase PknB is essential for growth and survival of the
pathogen in vitro and in vivo. Here we report the results of our efforts to elucidate the mechanism …
pathogen in vitro and in vivo. Here we report the results of our efforts to elucidate the mechanism …
Deciphering kinase–substrate relationships by analysis of domain-specific phosphorylation network
Motivation: In silico prediction of site-specific kinase–substrate relationships (ssKSRs) is
crucial for deciphering phosphorylation networks by linking kinomes to phosphoproteomes. …
crucial for deciphering phosphorylation networks by linking kinomes to phosphoproteomes. …