[HTML][HTML] Multiple sclerosis and myelin basic protein: Insights into protein disorder and disease

V Martinsen, P Kursula - Amino Acids, 2022 - Springer
Myelin basic protein (MBP) is an abundant protein in central nervous system (CNS) myelin.
MBP has long been studied as a factor in the pathogenesis of the autoimmune …

[HTML][HTML] Arginine methylation: an emerging regulatorof protein function

MT Bedford, S Richard - Molecular cell, 2005 - cell.com
Arginine methylation is now coming out of the shadows of protein phosphorylation and
entering the mainstream, largely due to the identification of the family of enzymes that lay …

[HTML][HTML] Myelin proteomics: molecular anatomy of an insulating sheath

O Jahn, S Tenzer, HB Werner - Molecular neurobiology, 2009 - Springer
Fast-transmitting vertebrate axons are electrically insulated with multiple layers of
nonconductive plasma membrane of glial cell origin, termed myelin. The myelin membrane …

[HTML][HTML] The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis

MA Moscarello, FG Mastronardi, DD Wood - Neurochemical research, 2007 - Springer
The pathogenesis of MS is unknown. In our studies, we have demonstrated an important
role for citrullinated myelin basic protein (MBP). The accompanying loss of positive charge …

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

G Harauz, N Ishiyama, CMD Hill, IR Bates, DS Libich… - Micron, 2004 - Elsevier
The 18.5 kDa isoform of myelin basic protein (MBP) is a major component of the myelin
sheath in the central nervous system of higher vertebrates, and a member of a larger family …

Increased citrullination of histone H3 in multiple sclerosis brain and animal models of demyelination: a role for tumor necrosis factor-induced peptidylarginine …

FG Mastronardi, DD Wood, J Mei… - Journal of …, 2006 - Soc Neuroscience
Modification of arginine residues by citrullination is catalyzed by peptidylarginine
deiminases (PADs), of which five are known, generating irreversible protein structural …

Structural polymorphism and multifunctionality of myelin basic protein

G Harauz, V Ladizhansky, JM Boggs - Biochemistry, 2009 - ACS Publications
Central nervous system myelin is a dynamic entity arising from membrane processes
extended from oligodendrocytes, which form a tightly wrapped multilamellar structure …

Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene …

S Chavanas, MC Méchin, H Takahara, A Kawada… - Gene, 2004 - Elsevier
Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines.
They are suspected to be involved in multiple sclerosis and rheumatoid arthritis …

Myelin management by the 18.5‐kDa and 21.5‐kDa classic myelin basic protein isoforms

G Harauz, JM Boggs - Journal of neurochemistry, 2013 - Wiley Online Library
The classic myelin basic protein (MBP) splice isoforms range in nominal molecular mass
from 14 to 21.5 kDa, and arise from the gene in the oligodendrocyte lineage (Golli) in …

Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation

P Proost, T Loos, A Mortier, E Schutyser… - The Journal of …, 2008 - rupress.org
Biological functions of proteins are influenced by posttranslational modifications such as
on/off switching by phosphorylation and modulation by glycosylation. Proteolytic processing …