Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Joanna K. Nagy"'
Autor:
Joanna K. Nagy, Charles R. Sanders
Publikováno v:
Biochemistry. 43:19-25
In this work, the relationship between stability and propensity to misfold was probed for a series of purified variants of the polytopic integral membrane protein diacylglycerol kinase. It was observed that there was a strong correlation between stab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c9619eaefced9213b4cf959caaefbab
https://doi.org/10.1021/bi035918s
https://doi.org/10.1021/bi035918s
Autor:
Charles R. Sanders, Joanna K. Nagy
Publikováno v:
Biochemistry. 41:9021-9025
Although a number of common diseases are a direct consequence of membrane protein misfolding, studies of membrane protein folding and misfolding lag well behind those of soluble proteins. Here it is shown that an interfacial residue, Tyr16, of the in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fb615eba1214b77bbc47a2dee46cbf9
https://doi.org/10.1021/bi020318z
https://doi.org/10.1021/bi020318z
Publikováno v:
Biochemistry. 40:8971-8980
Despite the relevance of membrane protein misfolding to a number of common diseases, our understanding of the folding and misfolding of membrane proteins lags well behind soluble proteins. Here, the overall kinetics of membrane insertion and folding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::168e058b3ebf540067d75becfefa10c3
https://doi.org/10.1021/bi010202n
https://doi.org/10.1021/bi010202n
Autor:
Charles R. Sanders, Joanna K. Nagy
Publikováno v:
Current Opinion in Structural Biology. 10:438-442
Protein misfolding is increasingly recognized as a factor in many diseases, including cystic fibrosis, Parkinson's, Alzheimer's and atherosclerosis. Many proteins involved in misfolding-based pathologies are membrane-associated, such that the bilayer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::943ea728da87c899de1930deeded306a
https://doi.org/10.1016/s0959-440x(00)00112-3
https://doi.org/10.1016/s0959-440x(00)00112-3
Autor:
Melvin H. Keyes, Charles R. Sanders, Amy Kuhn Hoffmann, Joanna K. Nagy, Don N. Gray, Kirill Oxenoid
Publikováno v:
FEBS letters. 501(2-3)
Data are presented which suggest that a class of amphiphilic polymers known as ‘amphipols’ may serve as a vehicle for delivering complex integral membrane proteins into membranes. The integral membrane protein diacylglycerol kinase (DAGK) was mai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c10cef2b24b0660aa71a2805e2d87889
https://pubmed.ncbi.nlm.nih.gov/11470268
https://pubmed.ncbi.nlm.nih.gov/11470268
Autor:
Carlos A. Muro-Cacho, Mark W. Wagner, Terry J. Hassold, Joanna K. Nagy, Antonio Gualberto, Mary L. Hixon, Carlos A. Obejero-Paz, Elise Millie
Publikováno v:
The Journal of biological chemistry. 275(51)
Vascular smooth muscle cells (VSMC) at capacitance arteries of hypertensive individuals and animals undergo dramatic polyploidization that contributes toward their hypertrophic phenotype. We report here the identification of a defective mitotic spind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8577c8f79daa70fab0eb10108de5b61
https://pubmed.ncbi.nlm.nih.gov/11005810
https://pubmed.ncbi.nlm.nih.gov/11005810
Publikováno v:
Biochemistry. 39(14)
This work represents the first stage of thiol-based cross-linking studies to map the oligomeric interface of the homotrimeric membrane protein diacylglycerol kinase (DAGK). A total of 53 single-cysteine mutants spanning DAGK's three transmembrane seg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e349705a1221ed0942c2b0d13eef1db
https://pubmed.ncbi.nlm.nih.gov/10747807
https://pubmed.ncbi.nlm.nih.gov/10747807
Autor:
Willis L. Lonzer, Joanna K. Nagy, David S. Cafiso, Kirill Oxenoid, Bonnie M. Gorzelle, Charles R. Sanders
Publikováno v:
Biochemistry. 38(49)
While the formation of kinetically trapped misfolded structural states by membrane proteins is related to a number of diseases, relatively few studies of misfolded membrane proteins in their purified state have been carried out and few methods for re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c012fddf5b812c69ed0b3a1ae3e2a3a
https://pubmed.ncbi.nlm.nih.gov/10587463
https://pubmed.ncbi.nlm.nih.gov/10587463