Author

Erin Skeens

Brown UniversityORCID 0000-0002-0580-1291Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Approach:biophysical modeling· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

George P. LisiiD· 3 shared Anton M. BennettiD· 2 shared Elias J. LolisiD· 2 shared Ramu ManjulaiD· 2 shared Aakash SahaiD· 1 shared Alexa L KnightiD· 1 shared Charlotte S Dresser· 1 shared David Ward TayloriD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiochemistry

George P. LisiORCID

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3 papers

Recent·Most cited

A Cryptic Binding Pocket Regulates the Metal-Dependent Activity of Cas9

Mohd Ahsan, Alexa L Knight, Aakash Saha, Delisa Ramos, Isabel Strohkendl, Erin Skeens, M. Stewart West, Jinping Luo, Charlotte S Dresser, David Ward Taylor, George P. Lisi, Giulia Palermo

This study identifies a cryptic divalent metal binding pocket that regulates Cas9's metal-dependent activity through conformational activation and catalytic efficiency.

Nature Communications · Oct 9, 2026Peer-reviewedBiophysics

Functional coupling between the a4 - a5 loop and allosteric site on MKP5 is a critical determinant of catalysis

R. Manjula, Lubna Ghanem, Erin Skeens, Leanna Bai, George P. Lisi, Elias Lolis, Anton M. Bennett

The paper investigates how structural changes in the 4-5 loop of MKP5 affect its catalytic activity and shows that mutations in this loop and adjacent regions disrupt enzyme function.

bioRxiv · Jun 2, 2026 · PreprintBiochemistry

Dynamic and structural insights into allosteric regulation on MKP5 a dual-specificity phosphatase

Erin Skeens, Federica Maschietto, Ramu Manjula, Shanelle R. Shillingford, James Murphy, Elias J. Lolis, Víctor S. Batista, Anton M. Bennett, George P. Lisi

This study investigates the allosteric regulation of MKP5 by identifying the role of residue Y435 in maintaining the structural integrity of the allosteric pocket and its interaction with p38 MAPK and JNK.

Nature Communications · Jul 31, 2025Peer-reviewedBiochemistry