Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Kenrick A Vassall"'
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e68175 (2013)
The classic isoforms of myelin basic protein (MBP) are essential for the formation and maintenance of myelin in the central nervous system of higher vertebrates. The protein is involved in all facets of the development, compaction, and stabilization
Externí odkaz:
https://doaj.org/article/5643ad5ce2cf4827b9bbfa4471a29d45
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 85:1336-1350
The molecular details of the association between the human Fyn-SH3 domain, and the fragment of 18.5-kDa myelin basic protein (MBP) spanning residues S38-S107 (denoted as xα2-peptide, murine sequence numbering), were studied in silico via docking and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::412adac8ed95a55ee0650c97367f8059
https://doi.org/10.1002/prot.25295
https://doi.org/10.1002/prot.25295
Autor:
Caroline Velte, Dariush Hinderberger, George Harauz, Kenrick A. Vassall, Daniel R. Kattnig, Andrew D. Jenkins, Vladimir V. Bamm, Joan M. Boggs
Publikováno v:
BASE-Bielefeld Academic Search Engine
Intrinsically-disordered proteins (IDPs) present a complex interplay of conformational variability and multifunctionality, modulated by environment and post-translational modifications. The 18.5-kDa myelin basic protein (MBP) is essential to the form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e41c39a46324b03a6a3c23dedb37623
https://doi.org/10.1016/j.bbamem.2016.02.024
https://doi.org/10.1016/j.bbamem.2016.02.024
Publikováno v:
Protein Science. 24:2081-2089
Neurotoxic misfolding of Cu, Zn‐superoxide dismutase (SOD1) is implicated in causing amyotrophic lateral sclerosis, a devastating and incurable neurodegenerative disease. Disease‐linked mutations in SOD1 have been proposed to promote misfolding a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75c366effb7c73a6fe4d4bdec5092414
https://doi.org/10.1002/pro.2803
https://doi.org/10.1002/pro.2803
Publikováno v:
Journal of Molecular Biology. 427:1977-1992
The intrinsically disordered, 18.5-kDa isoform of myelin basic protein (MBP) is a peripheral membrane protein that is essential to proper myelin formation in the central nervous system. MBP acts in oligodendrocytes both to adjoin membrane leaflets to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc381f1ef293bedc3ed088fb126977f6
https://doi.org/10.1016/j.jmb.2015.03.011
https://doi.org/10.1016/j.jmb.2015.03.011
Publikováno v:
SURG Journal. 7:30-41
Myelin Basic Protein (MBP) is a highly abundant protein in central nervous system (CNS) myelin that has a critical role in its proper formation and functioning. The 21.5-kDa isoform of MBP has been shown to be selectively imported into the nucleus of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4380678b25ee9c466f0ab93b2c8616e0
https://doi.org/10.21083/surg.v7i3.2958
https://doi.org/10.21083/surg.v7i3.2958
Publikováno v:
Proteins. 85(7)
The molecular details of the association between the human Fyn-SH3 domain, and the fragment of 18.5-kDa myelin basic protein (MBP) spanning residues S38-S107 (denoted as xα2-peptide, murine sequence numbering), were studied in silico via docking and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::97c5b37fee9b746d8da8989d42da0681
https://pubmed.ncbi.nlm.nih.gov/28380689
https://pubmed.ncbi.nlm.nih.gov/28380689
Autor:
Jessica A.O. Rumfeldt, Johnathan J. Almey, Helen R. Broom, Elizabeth M. Meiering, Peter B. Stathopulos, Colleen M. Doyle, Kenrick A. Vassall, Aron Broom
Publikováno v:
Archives of Biochemistry and Biophysics. 531:44-64
In nature, proteins most often exist as complexes, with many of these consisting of identical subunits. Understanding of the energetics governing the folding and misfolding of such homooligomeric proteins is central to understanding their function an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b90a9a8c292c5591a2517d8802e3bae
https://doi.org/10.1016/j.abb.2012.12.005
https://doi.org/10.1016/j.abb.2012.12.005
Autor:
Kenrick A. Vassall, Ming Sze Tong, Helen R. Broom, Colleen M. Doyle, Elizabeth M. Meiering, Jessica A.O. Rumfeldt, Julia Maeve Bonner
Publikováno v:
Biochemistry. 55(3)
Many proteins are naturally homooligomers, homodimers most frequently. The overall stability of oligomeric proteins may be described in terms of the stability of the constituent monomers and the stability of their association; together, these stabili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1988bc0aaca7f415ba05b48a1e929c4
https://pubmed.ncbi.nlm.nih.gov/26710831
https://pubmed.ncbi.nlm.nih.gov/26710831
Publikováno v:
The Biochemical journal. 472(1)
The classic isoforms of myelin basic protein (MBP, 14–21.5 kDa) are essential to formation of the multilamellar myelin sheath of the mammalian central nervous system (CNS). The predominant 18.5-kDa isoform links together the cytosolic surfaces of o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ddc5e96565e5db35793ee83490454f6
https://pubmed.ncbi.nlm.nih.gov/26518750
https://pubmed.ncbi.nlm.nih.gov/26518750