Zobrazeno 1 - 10
of 151
pro vyhledávání: '"Joseph Horwitz"'
Autor:
Daniel J. Blackstock, Alvenne Goh, Shamitha Shetty, Giulia Fabozzi, Rong Yang, Vera B. Ivleva, Richard Schwartz, Joseph Horwitz
Publikováno v:
Research, Vol 2020 (2020)
The generation of stable clones for biomolecule production is a common but lengthy and labor-intensive process. For complex molecules, such as viruses or virus-like particles (VLPs), the timeline becomes even more cumbersome. Thus, in the early stage
Externí odkaz:
https://doaj.org/article/74afee2ea54c4429a0e2b8eaa6ece7ef
Autor:
Katia Lopez, Kate Liu, Joseph Horwitz, Harrison Shawa, Rebeccah A. Warmack, Steven Clarke, Joseph A. Loo
Publikováno v:
J Biol Chem
Transparency in the lens is accomplished by the dense packing and short-range order interactions of the crystallin proteins in fiber cells lacking organelles. These features are accompanied by a lack of protein turnover, leaving lens proteins suscept
Autor:
J Andrew, Aquilina, Justin L P, Benesch, Lin Lin, Ding, Orna, Yaron, Joseph, Horwitz, Carol V, Robinson
The small heat shock protein, alpha-crystallin, plays a key role in maintaining lens transparency by chaperoning structurally compromised proteins. This is of particular importance in the human lens, where proteins are exposed to post-translational m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::894c714aa712524dee8b24cd8153c5d1
https://doi.org/10.1074/jbc.m500135200
https://doi.org/10.1074/jbc.m500135200
Publikováno v:
Journal of Biological Chemistry. 287:42407-42416
αA-Crystallin (αA) and αB-crystallin (αB), the two prominent members of the small heat shock family of proteins are considered to be two subunits of one multimeric protein, α-crystallin, within the ocular lens. Outside of the ocular lens, howeve
Autor:
J. Andrew Aquilina, Joseph Horwitz, Orna Yaron, Justin L. P. Benesch, Carol V. Robinson, Lin Lin Ding
Phosphorylation is the most common posttranslational modification of the alpha-crystallins in the human lens. These phosphorylated forms are not only important because of their abundance in aging lenses and the implications for cataract but also beca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::794557fd05ecaccf61f9688203052ae1
https://ora.ox.ac.uk/objects/uuid:a3202763-fb91-4fbb-ad21-f9e6ab58160c
https://ora.ox.ac.uk/objects/uuid:a3202763-fb91-4fbb-ad21-f9e6ab58160c
Autor:
John A. Carver, Elizabeth Vierling, Andrew Baldwin, Glyn L. Devlin, Agata Rekas, Justin L. P. Benesch, Eman Basha, Florian Stengel, Carol V. Robinson, J. Andrew Aquilina, Joseph Horwitz, Robyn A. Lindner
SummaryThe function of ScHSP26 is thermally controlled: the heat shock that causes the destabilization of target proteins leads to its activation as a molecular chaperone. We investigate the structural and dynamical properties of ScHSP26 oligomers th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e32dc96a60ea2b110db0fe0314992410
https://ora.ox.ac.uk/objects/uuid:194c62c3-2d41-4e1f-8956-a003b3448fcd
https://ora.ox.ac.uk/objects/uuid:194c62c3-2d41-4e1f-8956-a003b3448fcd
Autor:
Justin L. P. Benesch, Duilio Cascio, Qingling Huang, David Eisenberg, Carol V. Robinson, Meytal Landau, Michael R. Sawaya, Joseph Horwitz, Linlin Ding, Arthur Laganowsky
Publikováno v:
Protein Science. 19:1031-1043
Small heat shock proteins alphaA and alphaB crystallin form highly polydisperse oligomers that frustrate protein aggregation, crystallization, and amyloid formation. Here, we present the crystal structures of truncated forms of bovine alphaA crystall
Autor:
Joseph Horwitz
Publikováno v:
Experimental Eye Research. 88:190-194
Alpha A and alpha B crystallins are key members of the small heat-shock protein family. In addition to being a major structural protein of the lens, they are constitutively found in many other cells, where their function to is not completely understo
Autor:
Ronald H. P. H. Smulders, Karin B. Merck, John Aendekerk, Joseph Horwitz, Larry Takemoto, Christine Slingsby, Hans Bloemendal, Wilfried W. Jong
Publikováno v:
European Journal of Biochemistry. 232:834-838
Publikováno v:
Biochemistry. 45:1470-1479
The bacterial Na(+)/galactose cotransporter vSGLT of Vibrio parahaemolyticus is a member of the sodium:solute symporter family (SSS). Previous studies using electron microscopy have shown that vSGLT is a monomeric protein. Computational and experimen