Author

J. L. M. Kotler

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· 2

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:protein sequence· 2 Assay:protein structure· 2 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

T. O. Street· 2 shared B. Huang· 1 shared E. E. Deans· 1 shared J. C. Halpin· 1 shared S. Wang· 1 shared W.-S. Wei· 1 shared Y. Jin· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

7 top collaborators · 13 mutual co-author links

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2 shared papersBiochemistry

T. O. Street

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2 papers

Recent·Most cited

BiochemistrybioRxivPreprintOct 11, 2021

Electrostatics cause the molecular chaperone BiP to preferentially bind oligomerized states of a client protein

J. L. M. Kotler, W.-S. Wei, E. E. Deans, T. O. Street

This study shows that electrostatic interactions enable BiP to preferentially bind oligomeric states of proIGF2 over monomers.

DOI 10.1101/2021.10.11.463904

protein structureprotein sequence

𝕏 PostBluesky

BiochemistrybioRxivSep 24, 2020

The ER chaperones BiP and Grp94 regulate the formation of insulin-like growth factor 2 (IGF2) oligomers

Y. Jin, J. L. M. Kotler, S. Wang…·T. O. Street

This study shows that ER chaperones BiP and Grp94 regulate proIGF2 folding and oligomerization, with BiP suppressing and Grp94 enhancing oligomerization under different ATP/ADP conditions.

DOI 10.1016/j.jmb.2021.166963

protein structureprotein sequence

𝕏 PostBluesky