Author

J. D. Gross

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· 2 Biophysics· 2 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 5 Research Focus:chromatin & epigenetic regulation· 3 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:ChIP-seq· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

R. W. Tibble· 3 shared J. H. Lobel· 2 shared V. L. Lam· 2 shared A. Cruz· 1 shared A. J. Samelson· 1 shared A. L. Burlingame· 1 shared A. Vallejo-Gracia· 1 shared B. D. Pascal· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 13 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 papersBiophysics

R. W. Tibble

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis

A. J. Samelson, N. Ariqat, J. McKetney, G. Rohanitazangi, C. Parra Bravo, R. Bose, K. J. Travaglini, V. L. Lam, D. Goodness, G. Dixon, E. Marzette, J. Jin, R. Tian, E. Tse, R. Abskharon, , M. Kampmann

The paper uses CRISPR screens in iPSC-derived neurons to identify factors controlling tau aggregation, finding new pathways and potential therapeutic targets for tauopathies.

bioRxiv · Jun 16, 2023Cell Biology

SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein

M. Walter, I. P. Chen, A. Vallejo-Gracia, I.-J. Kim, O. Bielska, V. L. Lam, J. M. Hayashi, A. Cruz, S. Shah, J. D. Gross, N. J. Krogan, B. Schilling, M. Ott, E. Verdin

This study identifies SIRT5 as a proviral factor that interacts with SARS-CoV-2 Nsp14, enhancing viral replication and suggesting it as a therapeutic target.

bioRxiv · Jan 4, 2022Microbiology

Structure of the poxvirus decapping enzyme D9 reveals its mechanism of cap recognition and catalysis

J. K. Peters, R. W. Tibble, M. Warminski, J. Jemielity, J. D. Gross

The paper determines the structure of the poxvirus decapping enzyme D9, revealing its mechanism for recognizing and catalyzing the removal of the 5' cap from mRNA.

bioRxiv · Oct 4, 2021Biophysics

Pat1 increases the range of decay factors and RNA bound by the Lsm1-7 complex

J. H. Lobel, J. D. Gross

The paper shows Pat1 enhances Lsm1-7 binding to RNA by increasing cooperativity and multimerization, broadening RNA specificity.

bioRxiv · Apr 7, 2020Biochemistry

Pat1 activates late steps in mRNA decay by multiple mechanisms

J. H. Lobel, R. W. Tibble, J. D. Gross

This study reveals how Pat1 coordinates the assembly and activation of a decapping mRNP to promote 5-3 mRNA degradation through multiple mechanisms.

bioRxiv · Mar 30, 2019Biochemistry

Disorganization of the histone core promotes organization of heterochromatin into phase-separated droplets

S. Sanulli, M. J. Trnka, V. Dharmarajan, R. W. Tibble, B. D. Pascal, A. L. Burlingame, P. R. Griffin, J. D. Gross, G. J. Narlikar

This study shows that the S. pombe HP1 protein Swi6 promotes chromatin compaction through phase-separated droplets by disorganizing the histone core and increasing histone residue accessibility.

bioRxiv · Nov 18, 2018 · PreprintBiophysics