Author

D. Karandur

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

Biology Disciplines

Click to filter author papers

Biochemistry· 4 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 4 Assay:proteomics· 4 Organism:human· 3 Approach:biophysical modeling· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1

Frequent Co-Authors

J. Kuriyan· 3 shared N. H. Shah· 3 shared A. E. van Vlimmeren· 2 shared Z. Jiang· 2 shared A. Merk· 1 shared A. Semmelman· 1 shared C. A. Chartier· 1 shared C. J. Huang· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

J. Kuriyan

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Deep mutational scanning of a multi-domain signaling protein reveals mechanisms of regulation and pathogenicity

Z. Jiang, A. E. van Vlimmeren, D. Karandur, A. Semmelman, N. H. Shah

The paper uses deep mutational scanning to analyze SHP2 mutations, revealing diverse regulatory mechanisms and potential pathogenicity of uncharacterized variants.

bioRxiv · May 13, 2024 · PreprintBiochemistry

The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain

A. E. van Vlimmeren, R. Voleti, C. A. Chartier, Z. Jiang, D. Karandur, P. A. Humphries, W.-L. Lo, N. H. Shah

This paper investigates the T42A mutation in SHP2, showing it alters ligand-binding specificity in the N-terminal SH2 domain, leading to biased activation and enhanced signaling.

bioRxiv · Jul 10, 2023Biochemistry

A Saturation-Mutagenesis Analysis of the Interplay Between Stability and Activation in Ras

F. Hidalgo, L. M. Nocka, N. H. Shah, K. Gorday, N. R. Latorraca, P. Bandaru, S. Templeton, D. Lee, D. Karandur, J. G. Pelton, S. Marqusee, D. Wemmer, J. Kuriyan

This study shows that cancer hotspot mutations in Ras activate it regardless of stability, while non-hotspot mutations can be activating or deleterious depending on stability.

bioRxiv · Jan 6, 2022Biophysics

A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor

Y. Huang, J. Ognjenovic, D. Karandur, K. Miller, A. Merk, S. Subramaniam, J. Kuriyan

This study identifies how EGFR differentiates signaling outputs from EGF and TGF- through conformational changes in its extracellular domain.

bioRxiv · Dec 8, 2020Biochemistry

CRISPR-Cas12a exploits R-loop asymmetry to form double strand breaks

J. C. Cofsky, D. Karandur, C. J. Huang, I. P. Witte, J. Kuriyan, J. A. Doudna

This study shows that Cas12a uses R-loop asymmetry to cut the second DNA strand without direct protein interaction, explaining its double-strand break mechanism.

bioRxiv · Feb 10, 2020Biochemistry