Author

Kirsten J. Lampi

Oregon Health & Science UniversityORCID 0000-0002-7906-6699Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Biophysics· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:electronic health records· 1 Approach:experimental assay· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Assay:protein structure· 1

Frequent Co-Authors

Adam P. MilleriD· 1 shared Calvin Vetter· 1 shared Elisar J. BarbariD· 1 shared Heather M. Forsythe· 1 shared Kayla Ann JaraiD· 1 shared Larry L. David· 1 shared Patrick N. ReardoniD· 1 shared Steve ReichowiD· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 18 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

1 shared paperBiophysics

Adam P. MillerORCID

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

BiophysicsJournal of Molecular BiologyPeer-reviewedAug 17, 2023

The α-crystallin chaperones undergo a quasi-ordered co-aggregation process in response to saturating client interaction

Adam P. Miller, Susan E. O'Neill, Kirsten J. Lampi, Steve Reichow

This study examines how α-crystallin chaperones undergo structured co-aggregation when interacting with clients, revealing a quasi-ordered process distinct from amorphous aggregation.

16 citations

electronic health recordsbiophysical modeling

𝕏 PostBluesky

BiophysicsbioRxivPreprintMay 22, 2019

Cataract-associated deamidations on the surface of γS-crystallin increase protein unfolding and flexibility at distant regions

Heather M. Forsythe, Calvin Vetter, Kayla Ann Jara…·Kirsten J. Lampi

This study identifies deamidation sites in γS-crystallin that increase protein dynamics and flexibility in distant regions, contributing to cataract formation.

DOI 10.1101/646083

humanprotein structure

𝕏 PostBluesky