Results 291 to 300 of about 5,666,125 (336)

Intrinsic myelin proteins are normally synthesized in vitro in the myelin-deficient (mld) mutant mouse.

Developmental Neuroscience, 1983
The synthesis of myelin basic protein is severely reduced in the central and peripheral nervous system of myelin-deficient (mld) mutant mice. Using an in vitro system and immunoprecipitation, we found a normal rate of synthesis in mld mice for two ...
J. Matthieu, G. Almazan, T. Waehneldt
semanticscholar   +1 more source

Myelin basic protein interacts with the myelin-specific ganglioside GM4

Brain Research, 1981
Demyelinated plaques in multiple sclerosis have decreased amounts of both myelin basic protein and sialosylgalactosylceramide (GM4), a ganglioside specifically localized in myelin and oligodendroglia of the central nervous system. We have found that myelin basic protein is capable of releasing large quantities of entrapped [14C]glucose from ...
Francis X. Decandis, John D. Reid, Anthony J. Montanaro, Brian R. Mullin   +3 more
openaire   +3 more sources

The turnover of myelin proteins in adult rat brain.

International Journal of Neuroscience, 1979
The turnover of proteins of myelin of brain was followed after an intracerebral injections of [1-14C] leucine into adult rats and compared with the turnover of proteins of total brain homogenate, microsomal and supernatant fractions.
H. Singh, F. Jungalwala
semanticscholar   +1 more source

Myelin basic protein: a multifunctional protein

Cellular and Molecular Life Sciences, 2006
Myelin basic protein (MBP), the second most abundant protein in central nervous system myelin, is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. A member of the 'intrinsically disordered' or conformationally adaptable protein family, it also appears to have several other functions.
Joan M. Boggs, Joan M. Boggs
openaire   +3 more sources

Myelin‐specific proteolipid protein is expressed in myelinating schwann cells but is not incorporated into myelin sheaths

Journal of Neuroscience Research, 1987
AbstractContrary to widely held beliefs, the gene encoding proteolipid protein (PLP), the major structural protein of central nervous system myelin, is ecpressed in Schwann cells and their tumors. Proteolipid mRNA was identified in human acoustic neuromas and in rat and rabbit sciatic nerves using a human PLP cDNA as probe.
Lynn D. Hudson, Monique Dubois-Dalcq, K Ono, Robert A. Lazzarini, C Puckett, V Friedrich, J Benecke   +6 more
openaire   +3 more sources

Many facets of the peripheral myelin protein PMP22 in myelination and disease

Microscopy Research and Technique, 1998
Peripheral myelin protein 22 (PMP22) is a small, hydrophobic glycoprotein, which is most prominently expressed by Schwann cells as a component of compact myelin of the peripheral nervous system (PNS). Recent progress in molecular genetics revealed that mutations affecting the PMP22 gene including duplications, deletions, and point mutations are ...
Ueli Suter, Roland Naef
openaire   +3 more sources

Partial deficiencies in the myelin proteins of developing mice heterozygous for the shiverer mutation.

, 1982
The central nervous system of the shiverer mouse is known to be severely deficient in myelin. Animals heterozygous for this autosomal-recessive mutation were crossed, and the myelin proteins were examined in the brains and spinal cords of shiverers and ...
W. Cammer
semanticscholar   +1 more source

Myelin Enzymes and Protein Metabolism

1972
Turnover of myelin has attracted interest in relation to clinical and experimental diseases involving demyelination (7, 11). In adult rats, myelin represents about 12 % of total fresh weight, of which some 25 % is protein (14) and earlier concepts for its relative inertness are difficult to reconcile with the known halflife of under 20 days for 90 % of
openaire   +3 more sources

Conformation of Myelin Basic Protein and Its Role in Myelin Formation

1978
High resolution 13C and 1H NMR spectra of myelin basic protein over a range of pH and concentrations indicate that intramolecular folding of the polypeptide chain occurs in aqueous solution in the region of residues 85 to 116. At pH 4 in D2O solution, the 13C resonances due to nonprotonated carbons of phenylalanine and tryptophan are broadened and ...
B. E. Chapman, W. J. Moore, L. T. Littlemore   +2 more
openaire   +3 more sources

From Myelin Basic Protein to Myelin Deficient Mice

1990
In order to control diseases affecting myelination, an understanding of normal myelin structure and its formation is essential. Paradoxically, much information about normal development can be obtained through investigations of hypomyelinated mutants.
J.-M. Matthieu, M. Tosic
openaire   +2 more sources