Author

H. Negi

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· 3 Plant Biology· 1

Signature Assays, Organisms & Methods

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Assay:proteomics· 4 Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Organism:human· 1 Organism:plant (other)· 1

Frequent Co-Authors

R. Das· 3 shared A. Ravichandran· 1 shared B. T. Mullis· 1 shared C. Patole· 1 shared D. S. Hembram· 1 shared D. Shet· 1 shared J. Roberts· 1 shared J. W. Stratmann· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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3 shared papersBiochemistry

R. Das

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Author profile →

4 papers

Recent·Most cited

Green leaf volatiles co-opt proteins involved in molecular pattern signaling in plant cells

S. Tanarsuwongkul, K. W. Fisher, B. T. Mullis, J. Roberts, H. Negi, Q. Wang, J. W. Stratmann

The paper shows GLVs induce similar early stress responses as DAMPs by altering phosphorylation of proteins involved in signaling pathways.

bioRxiv · Oct 15, 2022Plant Biology

Plasticity of the proteasome-targeting signal Fat10 enhances substrate degradation

H. Negi, A. Ravichandran, P. DasGupta, S. Reddy, R. Das

This study shows that the structural plasticity of the Fat10 proteasome-targeting tag enhances substrate degradation by creating partially unstructured regions and reducing resistance to mechanical unfolding.

bioRxiv · Jul 15, 2022Biochemistry

A novel polyubiquitin chain linkage formed by viral Ubiquitin prevents cleavage by deubiquitinating enzymes

H. Negi, P. P. Reddy, C. Patole, R. Das

This study identifies a unique viral ubiquitin that forms K54-linked polyubiquitin chains resistant to deubiquitinating enzymes and proteasomal degradation.

bioRxiv · Sep 4, 2019Biochemistry

The viral SUMO-targeted Ubiquitin Ligase ICP0 is phosphorylated and activated by host kinase Chk2

D. S. Hembram, H. Negi, P. Biswas, V. Tripathi, L. Bhushan, D. Shet, V. Kumar, R. Das

This study identifies how HSV's ICP0 protein uses phosphorylation by Chk2 to activate its SUMO-targeted Ubiquitin Ligase activity against PML NBs.

bioRxiv · Jul 21, 2019Biochemistry