Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Carolyn N. Kingsley"'
Autor:
Matthew A. Durst, Carolyn N. Kingsley, Benjamin E. Ramirez, Michael Caffrey, Helena L. Palka-Hamblin, Aleksandar Antanasijevic, Arnon Lavie
Publikováno v:
Journal of Biological Chemistry
Viral entry into host cells is mediated by membrane proteins in a metastable state that transition to a more stable state upon a stimulus. For example, in the influenza envelope protein hemagglutinin (HA), the low pH in the endosome triggers a transi
Autor:
Vijayalaxmi Gupta, Ernst Schönbrunn, Carolyn N. Kingsley, Joseph S. Tash, Xingxian Gu, Erick J. Carlson, Jon E. Hawkinson, Gunda I. Georg, Yan Yang, Jin-Yi Zhu
Publikováno v:
Chemmedchem
Analogues of N‐butyl‐1‐deoxynojirimycin (NB‐DNJ) were prepared and assayed for inhibition of ceramide‐specific glucosyltransferase (CGT), non‐lysosomal β‐glucosidase 2 (GBA2) and the lysosomal β‐glucosidase 1 (GBA1). Compounds 5 a
Autor:
Duncan J. Wardrop, Carolyn N. Kingsley, Michael Caffrey, Lijun Rong, Smanla Tundup, Aleksandar Antanasijevic, Balaji Manicassamy, Rama K. Mishra, Nicholas J. Hafeman
Publikováno v:
ACS Infectious Diseases. 2:608-615
The viral envelope protein hemagglutinin (HA) plays a critical role in influenza entry and thus is an attractive target for novel therapeutics. The small molecule tert-butylhydroquinone (TBHQ) has previously been shown to bind to HA and inhibit HA-me
Autor:
Domarin Khago, Chi-Yuan Cheng, Carolyn N. Kingsley, Kyle W. Roskamp, Rachel W. Martin, Kuo-Ying Huang, Songi Han, Ryan Sheil, Jan C. Bierma
Publikováno v:
J Am Chem Soc
We demonstrate that the effect of protein crowding is critically dependent on the stability of the protein’s hydration shell, which can dramatically vary between different proteins. In the human eye lens, γS-crystallin (γS-WT) forms a densely pac
Autor:
Arnab Basu, Lijun Rong, Aleksandar Antanasijevic, Carolyn N. Kingsley, Terry L. Bowlin, Michael Caffrey
Publikováno v:
Journal of Biomolecular NMR
The membrane proteins of viruses play critical roles in the virus life cycle and are attractive targets for therapeutic intervention. Virus Like Particles (VLP) present the possibility to study the biochemical and biophysical properties of viral memb
Autor:
J. Alfredo Freites, Douglas J. Tobias, Rachel W. Martin, Carolyn N. Kingsley, Domarin Khago, Eric K. Wong
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1860:325-332
Background The objective of this study was to determine whether the cataract-related G18V variant of human γ S-crystallin has increased exposure of hydrophobic residues that could explain its aggregation propensity and/or recognition by α B-crystal
Publikováno v:
The journal of physical chemistry. B, vol 118, iss 47
The Journal of Physical Chemistry. B
Kingsley, CN; Bierma, JC; Pham, V; & Martin, RW. (2014). γs-crystallin proteins from the antarctic nototheniid toothfish: A model system for investigating differential resistance to chemical and thermal denaturation. Journal of Physical Chemistry B, 118(47), 13544-13553. doi: 10.1021/jp509134d. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3h75g84j
The Journal of Physical Chemistry. B
Kingsley, CN; Bierma, JC; Pham, V; & Martin, RW. (2014). γs-crystallin proteins from the antarctic nototheniid toothfish: A model system for investigating differential resistance to chemical and thermal denaturation. Journal of Physical Chemistry B, 118(47), 13544-13553. doi: 10.1021/jp509134d. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3h75g84j
© 2014 American Chemical Society. The γS1- and γS2-crystallins, structural eye lens proteins from the Antarctic toothfish (Dissostichus mawsoni), are homologues of the human lens protein γS-crystallin. Although γS1 has the higher thermal stabili
Autor:
William D. Brubaker, Anne Diehl, Rachel W. Martin, Stefan Markovic, Carolyn N. Kingsley, Amanda J. Brindley, Hartmut Oschkinat
Publikováno v:
Structure (London, England : 1993), vol 21, iss 12
Structure, 21(12): 2221–2227
Structure, 21(12): 2221–2227
Transparency in the eye lens is maintained via specific, functional interactions among the structural βγ- and chaperone α-crystallins. Here we report the structure and α-crystallin binding interface of the G18V variant of human γS-crystallin (γ
Autor:
Kory J. Golchert, Shaul Mukamel, Carolyn N. Kingsley, Rachel W. Martin, Jun Jiang, William D. Brubaker
Publikováno v:
Jiang, J; Golchert, KJ; Kingsley, CN; Brubaker, WD; Martin, RW; & Mukamel, S. (2013). Exploring the aggregation propensity of γs-crystallin protein variants using two-dimensional spectroscopic tools. Journal of Physical Chemistry B, 117(46), 14294-14301. doi: 10.1021/jp408000k. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/6kw1f1c4
The journal of physical chemistry. B, vol 117, iss 46
The journal of physical chemistry. B, vol 117, iss 46
The formation of amyloid fibrils is associated with many serious diseases as well as diverse biological functions. Despite the importance of these aggregates, predicting the aggregation propensity of a particular sequence is a major challenge. We rep
Autor:
Chandra Srinivasan, Armando Durazo, William Munroe, Joan Selverstone Valentine, James A. Imlay, Edith Butler Gralla, Carolyn N. Kingsley
Publikováno v:
Journal of inorganic biochemistry. 101(11-12)
A variety of manganese-containing coordination compounds, frequently termed superoxide dismutase (SOD) mimics, have been reported to have SOD activity in vitro and to be effective at improving conditions related to increased oxidative stress in multi