Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Christopher J. McKnight"'
Autor:
Christopher J. McKnight
Publikováno v:
Journal of Technology Management & Innovation, Vol 1, Iss 5 (2006)
This document will cover the basics of Storage Area Networks (SAN), IP-Based Storage Networks such as NAS, and the basics of choosing a technology for an Enterprise Storage infrastructure. This document will focus on SAS (Serial Attached Storage) and
Externí odkaz:
https://doaj.org/article/0f9af09b77814f4d9578d63ded9710ea
Autor:
Aaron Griffin, Robert S. Hodges, Parker J. Nichols, Liliya Vugmeyster, Christopher J. McKnight, Beat Vögeli, Isaac B. Falconer, Colin T. Mant
Publikováno v:
Protein Sci
We have investigated the effect of deuteration of non‐exchangeable protons on protein global thermal stability, hydrophobicity, and local flexibility using well‐known thermostable model systems such as the villin headpiece subdomain (HP36) and th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29bb9fdd1283873977cb67841bda483e
https://europepmc.org/articles/PMC7314392/
https://europepmc.org/articles/PMC7314392/
Autor:
Stacy L. Chin, John E. Straub, Christopher J. McKnight, Qing Lu, Mark W. Grinstaff, Eric L. Dane, Laura Dominguez
Publikováno v:
Journal of the American Chemical Society. 138:6532-6540
Poly-amido-saccharides (PAS) are carbohydrate-based, enantiopure synthetic polymers in which sugar repeat units are joined by amide linkages. This unique and relatively rigid pyranose backbone contributes to their defined helical secondary structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3601f66c5b8a0e62b7b8aec034285be4
https://doi.org/10.1021/jacs.6b01837
https://doi.org/10.1021/jacs.6b01837
Publikováno v:
Journal of the American Chemical Society. 139(40)
The design and synthesis of amide-linked saccharide oligomers and polymers, which are predisposed to fold into specific ordered secondary structures, is of significant interest. Herein, right-handed helical poly amido-saccharides (PASs) with β-N-(1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f25d1b186d94c64d801c9891845a4840
https://pubmed.ncbi.nlm.nih.gov/28902504
https://pubmed.ncbi.nlm.nih.gov/28902504
Autor:
L. Burns, D.A. Pfaff, Serge L. Smirnov, Anton Sabantsev, Nelson A, Jacob A. Brockerman, Webb T, Fengli Zhang, Christopher J. McKnight, Alexei S. Melnikov, Stanislav O. Fedechkin
Publikováno v:
Biochemistry. 52:7890-7900
Villin is a gelsolin-like cytoskeleton regulator localized in the brush border at the apical end of epithelial cells. Villin regulates microvilli by bundling F-actin at low calcium levels and severing it at high calcium levels. The villin polypeptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::778c6dd48b867bdb6ba0de3dc494fc12
https://doi.org/10.1021/bi400699s
https://doi.org/10.1021/bi400699s
Publikováno v:
Arteriosclerosis, Thrombosis, and Vascular Biology. 33
High serum levels of low density lipoproteins (LDL) is associated with increased risk of atherosclerosis. Apolipoprotein B (ApoB) is required for the assembly and secretion of chylomicrons and very low density lipoproteins (VLDL), the precursor of lo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e10c3db56018aab3c56e68d9cf48a53a
https://doi.org/10.1161/atvb.33.suppl_1.a437
https://doi.org/10.1161/atvb.33.suppl_1.a437
Autor:
Jianmin Meng, Christopher J. McKnight
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 65(Pt 5)
The villin headpiece domain (HP67) is the C-terminal F-actin-binding motif that confers F-actin-bundling activity to villin, a component of the actin bundles that support the brush-border microvilli. It has been investigated extensively by both exper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a64907164952a38dd2c347c1f9bc099
https://pubmed.ncbi.nlm.nih.gov/19390152
https://pubmed.ncbi.nlm.nih.gov/19390152
Autor:
Christopher J. McKnight, J. Meng
Publikováno v:
Biochemistry. 47(16)
Villin-type headpiece domains are compact F-actin-binding motifs that have been used extensively as a model system to investigate protein folding by both experimental and computational methods. Villin headpiece (HP67) harbors a highly helical, thermo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d15b1381f64aa6cf19247eec2c51c86
https://pubmed.ncbi.nlm.nih.gov/18370407
https://pubmed.ncbi.nlm.nih.gov/18370407
Publikováno v:
Biochemistry. 46(25)
Villin is an F-actin regulating, modular protein with a gelsolin-like core and a distinct C-terminal ‘headpiece’ domain. Localized in the microvilli of the absorptive epithelium, villin can bundle F-actin and, at higher calcium concentration, is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55aa87d31b771344247b220178e6da4b
https://pubmed.ncbi.nlm.nih.gov/17547371
https://pubmed.ncbi.nlm.nih.gov/17547371
Publikováno v:
Biochemistry. 44(36)
Villin-type headpiece domains are approximately 70 amino acid modular motifs found at the C terminus of a variety of actin cytoskeleton-associated proteins. The headpiece domain of villin, a protein found in the actin bundles of the brush border epit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb6aa2d4a577ed22a8de1722b79daf0b
https://pubmed.ncbi.nlm.nih.gov/16142894
https://pubmed.ncbi.nlm.nih.gov/16142894