Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Kirsten J. Lampi"'
Autor:
Mason Posner, Kelly L. Murray, Matthew S. McDonald, Hayden Eighinger, Brandon Andrew, Amy Drossman, Zachary Haley, Justin Nussbaum, Larry L. David, Kirsten J. Lampi
Publikováno v:
PeerJ, Vol 5, p e4093 (2017)
Previous studies have used the zebrafish to investigate the biology of lens crystallin proteins and their roles in development and disease. However, little is known about zebrafish α-crystallin promoter function, how it compares to that of mammals,
Externí odkaz:
https://doaj.org/article/abdd6848761f44878ddc1cd8af63b96d
Publikováno v:
PLoS ONE, Vol 19, Iss 7, p e0306856 (2024)
Site-specific modifications of aspartate residues spontaneously occur in crystallin, the major protein in the lens. One of the primary modification sites is Asp151 in αA-crystallin. Isomerization and racemization alter the crystallin backbone struct
Externí odkaz:
https://doaj.org/article/9bac5b0f7b3a4e8ca8f302f56032cda6
Publikováno v:
Biophysical Journal. 122:38a
Autor:
Sidra Islam, Michael T. Do, Brett S. Frank, Grant L. Hom, Samuel Wheeler, Hisashi Fujioka, Benlian Wang, Geeta Minocha, David R. Sell, Xingjun Fan, Kirsten J. Lampi, Vincent M. Monnier
Publikováno v:
Journal of Biological Chemistry. 298:102417
Γ-Crystallins play a major role in age-related lens transparency. Their destabilization by mutations and physical chemical insults are associated with cataract formation. Therefore, drugs that increase their stability should have anticataract proper
Autor:
Kirsten J. Lampi, Elisar Barbar, Calvin Vetter, Kayla A. Jara, Heather M. Forsythe, Larry L. David, Patrick N. Reardon
Publikováno v:
Biochemistry. 58:4112-4124
Deamidation is a major age-related modification in the human lens that is highly prevalent in crystallins isolated from the insoluble fraction of cataractous lenses and also causes protein aggregation
Autor:
Maureen C Heaphy, Joseph L Harman, Gus D Warren, Kirsten J. Lampi, Andrea N. Loes, Michael J. Harms
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
Multifunctional proteins are evolutionary puzzles: how do proteins evolve to satisfy multiple functional constraints? S100A9 is one such multifunctional protein. It potently amplifies inflammation via Toll-like receptor four and is antimicrobial as p
Autor:
Calvin Vetter, Charlie C. Mundorff, Thomas E. Wales, John R. Engen, Kate Halverson, Samuel G. Wheeler, John A. Carver, Kirsten J. Lampi, Ujwal Shinde, David C. Thorn, Larry L. David
Publikováno v:
Protein Sci
Age-related lens cataract is the major cause of blindness worldwide. The mechanisms whereby crystallins, the predominant lens proteins, assemble into large aggregates that scatter light within the lens, and cause cataract, are poorly understood. Due
Autor:
Kirsten J. Lampi, Calvin Vetter, Charlie Mundorff, John A. Carver, Larry L. David, Kate Halverson, Samuel G. Wheeler, David C. Thorn
Age-related cataract is a major cause of blindness worldwide. Yet, the molecular mechanisms whereby large, light scattering aggregates form is poorly understood, because of the complexity of the aggregates isolated from human lenses. The predominant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1621f33ea650ba895af8e8bef14bb1ac
https://doi.org/10.1101/2020.02.21.960237
https://doi.org/10.1101/2020.02.21.960237
Autor:
Heather M. Forsythe, Kirsten J. Lampi, Larry L. David, Elisar Barbar, Kayla A. Jara, Patrick N. Reardon, Calvin Vetter
Deamidation is a major age-related modification in the human lens that is highly prevalent in crystallins isolated from cataractous lenses. However, the mechanism by which deamidation causes proteins to become insoluble is not known, because of only
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac25c7903637ad55cfa1b2f597bb6c72
https://doi.org/10.1101/646083
https://doi.org/10.1101/646083