View source for Myelin basic protein

{{Infobox_gene}}
{{Infobox protein family
| Symbol = Myelin_MBP
| Name = Myelin_MBP
| image = 
| width = 
| caption = 
| Pfam = PF01669
| Pfam_clan =  
| InterPro = IPR000548
| SMART = 
| PROSITE = PDOC00492
| MEROPS = 
| SCOP = 1bx2
| TCDB = 
| OPM family = 274
| OPM protein = 2lug
| CAZy = 
| CDD = 
}}
'''Myelin basic protein''' ('''MBP''') is a [[protein]] important in the process of [[myelination]] of [[nerve]]s in the [[nervous system]]. The [[myelin sheath]] is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of [[Action potential|axonal impulse conduction]].<ref name="pmid2435734">{{cite journal | vauthors = Sakamoto Y, Kitamura K, Yoshimura K, Nishijima T, Uyemura K | title = Complete amino acid sequence of PO protein in bovine peripheral nerve myelin | journal = The Journal of Biological Chemistry | volume = 262 | issue = 9 | pages = 4208–4214 | date = March 1987 | pmid = 2435734 | doi = 10.1016/S0021-9258(18)61334-1 | doi-access = free }}</ref> MBP  maintains the correct structure of myelin, interacting with the [[lipids]] in the myelin membrane.<ref name="pmid1710177">{{cite journal | vauthors = Deber CM, Reynolds SJ | title = Central nervous system myelin: structure, function, and pathology | journal = Clinical Biochemistry | volume = 24 | issue = 2 | pages = 113–134 | date = April 1991 | pmid = 1710177 | pmc = 7130177 | doi = 10.1016/0009-9120(91)90421-a }}</ref><ref name="pmid1710279">{{cite journal | vauthors = Inouye H, Kirschner DA | title = Folding and function of the myelin proteins from primary sequence data | journal = Journal of Neuroscience Research | volume = 28 | issue = 1 | pages = 1–17 | date = January 1991 | pmid = 1710279 | doi = 10.1002/jnr.490280102 | s2cid = 8598890 }}</ref>

MBP was initially [[sequencing|sequenced]] in 1971 after isolation from bovine myelin [[cell membrane|membrane]]s.<ref name="pmid5096093"/> MBP [[knockout mouse|knockout mice]] called [[Shiverer mouse|shiverer mice]] were subsequently developed and characterized in the early 1980s. ''Shiverer'' mice exhibit decreased amounts of CNS myelination and a progressive disorder characterized by [[tremor]]s, [[seizure]]s, and early death. The human [[gene]] for MBP is on [[chromosome 18]];<ref name="pmid2414074"/> the protein localizes to the CNS and to various [[cell (biology)|cell]]s of the [[Haematopoiesis|hematopoietic lineage]].

The pool of MBP in the [[central nervous system]] is very diverse, with several [[Alternative splicing|splice variants]] being expressed and a large number of [[post-translational modification]]s on the protein, which include [[phosphorylation]], [[methylation]], [[deamidation]], and [[citrullination]]. These forms differ by the presence or the absence of short (10 to 20 residues) peptides in various internal locations in the [[sequence (biology)|sequence]]. In general, the major form of MBP is a protein of about 18.5 Kd (170 residues).

In [[melanocytic cell]] types, MBP gene expression may be regulated by [[Microphthalmia-associated transcription factor|MITF]].<ref name="pmid19067971"/>

== Gene expression ==

The protein encoded by the classic ''MBP'' gene is a major constituent of the [[myelin]] sheath of [[oligodendrocyte]]s and [[Schwann cell]]s in the nervous system. However, MBP-related transcripts are also present in the bone marrow and the immune system. These [[messenger RNA|mRNAs]] arise from the long ''MBP'' gene (otherwise called "Golli-MBP") that contains three additional exons located upstream of the classic MBP exons. [[Alternative splicing]] from the Golli and the MBP transcription start sites gives rise to two sets of MBP-related transcripts and gene products. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. They encode hybrid proteins that have an [[N-terminus|N-terminal]] Golli amino acid sequence linked to the MBP amino acid sequence. The second family of transcripts contains only MBP exons and produces the well-characterized myelin basic proteins. This complex gene structure is conserved among species, suggesting that the MBP transcription unit is an integral part of the Golli transcription unit and that this arrangement is important for the function and/or regulation of these genes.<ref name="entrez">{{cite web | title = Entrez Gene: myelin basic protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4155}}</ref> At protein level, the concentration of MBP in the [[Central nervous system|CNS]] is tenfold higher in sections of [[white matter]] compared with [[cerebral cortex]].<ref>{{cite journal | vauthors = Sjölin K, Kultima K, Larsson A, Freyhult E, Zjukovskaja C, Alkass K, Burman J | title = Distribution of five clinically important neuroglial proteins in the human brain | journal = Molecular Brain | volume = 15 | issue = 1 | pages = 52 | date = June 2022 | pmid = 35765081 | pmc = 9241296 | doi = 10.1186/s13041-022-00935-6 | doi-access = free }}</ref>

== Structure ==

[[File:MBP Charge and Citrullination.png|thumb|left|MBP charge and citrullination|296x296px]]

Myelin basic protein has been classified as an [[Intrinsically disordered proteins|intrinsically disordered protein]] that has no stable secondary structure in solution.<ref>{{cite journal | vauthors = Anderson TR, Slotkin TA | title = Maturation of the adrenal medulla--IV. Effects of morphine | journal = Biochemical Pharmacology | volume = 24 | issue = 16 | pages = 1469–1474 | date = August 1975 | pmid = 7 | doi = 10.1016/0006-2952(75)90020-9 }}</ref> Like most IDPs, it has a high net charge and a low mean hydrophobicity, minimizing the hydrophobic effect that drives traditional protein folding. It does contain some exceptions to normal IDP amino acid content. For example, MBP has more arginine and less glutamic acid than most IDPs. However, this is likely because those changes are necessary for MBP to be sufficiently basic and positively charged to correctly interact with the membrane.<ref>{{cite journal | vauthors = Harauz G, Ishiyama N, Hill CM, Bates IR, Libich DS, Farès C | title = Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis | journal = Micron | volume = 35 | issue = 7 | pages = 503–542 | date = May 2004 | pmid = 15219899 | doi = 10.1016/s0968-4328(04)00096-4 }}</ref> Notably, MBP has been shown to adopt a more stable secondary structure on interaction with lipids.<ref>{{cite journal | vauthors = Moroi K, Sato T | title = Comparison between procaine and isocarboxazid metabolism in vitro by a liver microsomal amidase-esterase | journal = Biochemical Pharmacology | volume = 24 | issue = 16 | pages = 1517–1521 | date = August 1975 | pmid = 8 | doi = 10.1016/0006-2952(75)90029-5 }}</ref><ref>{{cite journal | vauthors = Marniemi J, Parkki MG | title = Radiochemical assay of glutathione S-epoxide transferase and its enhancement by phenobarbital in rat liver in vivo | journal = Biochemical Pharmacology | volume = 24 | issue = 17 | pages = 1569–1572 | date = September 1975 | pmid = 9 | doi = 10.1016/0006-2952(75)90080-5 }}</ref> [[Nuclear magnetic resonance|NMR]] and Cys-specific spin labeling experiments have predicted this structure to contain beta sheet and regions of [[Amphiphile|amphipathic]] helix.<ref>{{cite journal | vauthors = Bates IR, Feix JB, Boggs JM, Harauz G | title = An immunodominant epitope of myelin basic protein is an amphipathic alpha-helix | journal = The Journal of Biological Chemistry | volume = 279 | issue = 7 | pages = 5757–5764 | date = February 2004 | pmid = 14630913 | doi = 10.1074/jbc.m311504200 | doi-access = free }}</ref>

As implied by its name, myelin basic protein is significantly basic, with an [[isoelectric point]] of 10. It is thought to associate with the cell membrane through electrostatic interactions between its positive charges and negatively charged phospholipid heads of the plasma membrane.<ref name=":0" /> It can undergo a large variety of post-translational modifications, creating various charge isomers known as C1-C6 or C8.<ref>{{cite journal | vauthors = Zand R, Li MX, Jin X, Lubman D | title = Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectroscopy | journal = Biochemistry | volume = 37 | issue = 8 | pages = 2441–2449 | date = February 1998 | pmid = 9485392 | doi = 10.1021/bi972347t }}</ref> These modifications include [[phosphorylation]], [[methylation]], [[deamidation]], [[citrullination]], [[ADP-ribosylation]], and N-terminal [[acylation]] . C1 is the least modified, while C8 is the most distinct, containing 6-11 additional citrullinations. Since each of these decreases its positive charge, C8 has the smallest net positive charge of the isomers. Alternations in these post-translational modifications have been associated with [[Demyelinating disease|demyelinating diseases]]. Notably, MBP isolated from individuals with [[multiple sclerosis]] have had a higher degree of citrullination and a smaller positive charge. In a rare, severe form of MS known as Marburg's syndrome, the citrullination was even more extensive.<ref name=":0">{{cite journal | vauthors = Boggs JM | title = Myelin basic protein: a multifunctional protein | journal = Cellular and Molecular Life Sciences | volume = 63 | issue = 17 | pages = 1945–1961 | date = September 2006 | pmid = 16794783 | doi = 10.1007/s00018-006-6094-7 | s2cid = 1076002 | pmc = 11136439 }}</ref>

== Role in disease ==

Interest in MBP has centered on its role in [[demyelinating disease]]s, in particular, [[multiple sclerosis]] (MS). The target antigen of the autoimmune response in MS has not yet been identified.  However, several studies have shown a role for [[antibody|antibodies]] against MBP in the [[pathogenesis]] of MS.<ref name="pmid12853586"/> Some studies have linked a [[Genetics|genetic]] predisposition to MS to the MBP gene, though a majority have not.

A "molecular mimicry" hypothesis of multiple sclerosis has been suggested, in which [[T cells]] are, in essence, confusing MBP with [[human herpesvirus-6]]. Researchers in the United States created a synthetic peptide with a sequence identical to that of an HHV-6 peptide. Elevated levels of MBP have been found in the cerebrospinal fluid of patients with [[HIV]] infections and signs of encephalopathy, and although MBP does not seem to be a sensitive diagnostic marker of HIV encephalopathy, it has been suggested that it may serve a role as a prognostic indicator of disease progression.<ref name="pmid2474637">{{cite journal | vauthors = Pfister HW, Einhäupl KM, Wick M, Fateh-Moghadam A, Huber M, Schielke E, Goebel FD, Matuschke A, Heinrich B, Bogner JR | display-authors = 6 | title = Myelin basic protein in the cerebrospinal fluid of patients infected with HIV | journal = Journal of Neurology | volume = 236 | issue = 5 | pages = 288–291 | date = July 1989 | pmid = 2474637 | doi = 10.1007/bf00314458 | s2cid = 12178626 | url = http://nbn-resolving.de/urn:nbn:de:bvb:19-epub-7961-9 }}</ref> 
It is able to show that T cells were activated by this peptide. These activated T cells also recognized and initiated an immune response against a synthetically created peptide sequence that is identical to part of human MBP. During their research, they found that the levels of these cross-reactive T cells are significantly elevated in multiple sclerosis patients.<ref>{{cite journal | vauthors = Tejada-Simon MV, Zang YC, Hong J, Rivera VM, Zhang JZ | title = Cross-reactivity with myelin basic protein and human herpesvirus-6 in multiple sclerosis | journal = Annals of Neurology | volume = 53 | issue = 2 | pages = 189–197 | date = February 2003 | pmid = 12557285 | doi = 10.1002/ana.10425 | s2cid = 43317994 }}</ref>

[[File:HIV-induced autoimmun-antiMyelin Antibodies against human nerve tissue (FITC-Stain).jpg|left|thumb]]

Some research has shown that inoculating an animal with MBP to generate an MBP-specific immune response against it increases [[blood–brain barrier]] permeability. Permeability is enhanced when the animal is inoculated against non-specific proteins.<ref name="pmid7680933">{{cite journal | vauthors = Namer IJ, Steibel J, Poulet P, Armspach JP, Mohr M, Mauss Y, Chambron J | title = Blood-brain barrier breakdown in MBP-specific T cell induced experimental allergic encephalomyelitis. A quantitative in vivo MRI study | journal = Brain | volume = 116 ( Pt 1) | issue = 1 | pages = 147–159 | date = February 1993 | pmid = 7680933 | doi = 10.1093/brain/116.1.147 }}</ref>

A targeted immune response to MBP has been implicated in lethal [[rabies]] infection. The inoculation of MBP generates increases the permeability of the blood–brain barrier (BBB), allowing immune cells to enter the brain, the primary site of rabies virus replication. In a study of mice infected with Silver-haired bat rabies virus (SHBRV), the mortality rate of mice treated with MBP improved 20%-30% over the untreated control group. It is significant to note that healthy uninfected mice treated with MBP showed an increase in mortality rate between 0% and 40%.<ref name="pmid17507463"/>

== Interactions ==

Myelin basic protein has been shown to [[protein-protein interaction|interact]] ''in vivo'' with [[proteolipid protein 1]],<ref name="pmid6083474"/><ref name="pmid2467009"/> and ''in vitro'' with [[calmodulin]], [[actin]], [[tropomyosin]], [[tubulin]], [[clathrin]], [[2',3'-cyclic-nucleotide 3'-phosphodiesterase]] and multiple molecules of the [[immune system]].<ref>{{cite journal | vauthors = Harauz G, Ishiyama N, Hill CM, Bates IR, Libich DS, Farès C | title = Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis | journal = Micron | volume = 35 | issue = 7 | pages = 503–542 | year = 2004 | pmid = 15219899 | doi = 10.1016/j.micron.2004.04.005 }}</ref>{{clear}}

== References ==
{{Reflist | 32em | refs =

<ref name="pmid5096093">{{cite journal | vauthors = Eylar EH, Brostoff S, Hashim G, Caccam J, Burnett P | title = Basic A1 protein of the myelin membrane. The complete amino acid sequence | journal = The Journal of Biological Chemistry | volume = 246 | issue = 18 | pages = 5770–5784 | date = September 1971 | pmid = 5096093 | doi = 10.1016/S0021-9258(18)61872-1 | doi-access = free }}</ref>

<ref name="pmid2414074">{{cite journal | vauthors = Saxe DF, Takahashi N, Hood L, Simon MI | title = Localization of the human myelin basic protein gene (MBP) to region 18q22----qter by in situ hybridization | journal = Cytogenetics and Cell Genetics | volume = 39 | issue = 4 | pages = 246–249 | year = 1985 | pmid = 2414074 | doi = 10.1159/000132152 }}</ref>

<ref name="pmid19067971">{{cite journal | vauthors = Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E | display-authors = 6 | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell & Melanoma Research | volume = 21 | issue = 6 | pages = 665–676 | date = December 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x | s2cid = 24698373 | doi-access = free }}</ref>

<ref name="pmid12853586">{{cite journal | vauthors = Berger T, Rubner P, Schautzer F, Egg R, Ulmer H, Mayringer I, Dilitz E, Deisenhammer F, Reindl M | display-authors = 6 | title = Antimyelin antibodies as a predictor of clinically definite multiple sclerosis after a first demyelinating event | journal = The New England Journal of Medicine | volume = 349 | issue = 2 | pages = 139–145 | date = July 2003 | pmid = 12853586 | doi = 10.1056/NEJMoa022328 | doi-access = free }}</ref>

<ref name="pmid17507463">{{cite journal | vauthors = Roy A, Hooper DC | title = Lethal silver-haired bat rabies virus infection can be prevented by opening the blood-brain barrier | journal = Journal of Virology | volume = 81 | issue = 15 | pages = 7993–7998 | date = August 2007 | pmid = 17507463 | pmc = 1951307 | doi = 10.1128/JVI.00710-07 }}</ref>

<ref name="pmid6083474">{{cite journal | vauthors = Wood DD, Vella GJ, Moscarello MA | title = Interaction between human myelin basic protein and lipophilin | journal = Neurochemical Research | volume = 9 | issue = 10 | pages = 1523–1531 | date = October 1984 | pmid = 6083474 | doi = 10.1007/BF00964678 | s2cid = 9751765 }}</ref>

<ref name="pmid2467009">{{cite journal | vauthors = Edwards AM, Ross NW, Ulmer JB, Braun PE | title = Interaction of myelin basic protein and proteolipid protein | journal = Journal of Neuroscience Research | volume = 22 | issue = 1 | pages = 97–102 | date = January 1989 | pmid = 2467009 | doi = 10.1002/jnr.490220113 | s2cid = 33666906 }}</ref>

}}

== Further reading ==
{{refbegin|32em}}
* {{cite journal | vauthors = Boylan KB, Ayres TM, Popko B, Takahashi N, Hood LE, Prusiner SB | title = Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism | journal = Genomics | volume = 6 | issue = 1 | pages = 16–22 | date = January 1990 | pmid = 1689270 | doi = 10.1016/0888-7543(90)90443-X }}
* {{cite journal | vauthors = Kishimoto A, Nishiyama K, Nakanishi H, Uratsuji Y, Nomura H, Takeyama Y, Nishizuka Y | title = Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3':5'-monophosphate-dependent protein kinase | journal = The Journal of Biological Chemistry | volume = 260 | issue = 23 | pages = 12492–12499 | date = October 1985 | pmid = 2413024 | doi = 10.1016/S0021-9258(17)38898-1 | doi-access = free }}
* {{cite journal | vauthors = Saxe DF, Takahashi N, Hood L, Simon MI | title = Localization of the human myelin basic protein gene (MBP) to region 18q22----qter by in situ hybridization | journal = Cytogenetics and Cell Genetics | volume = 39 | issue = 4 | pages = 246–249 | year = 1985 | pmid = 2414074 | doi = 10.1159/000132152 }}
* {{cite journal | vauthors = Kamholz J, de Ferra F, Puckett C, Lazzarini R | title = Identification of three forms of human myelin basic protein by cDNA cloning | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 83 | issue = 13 | pages = 4962–4966 | date = July 1986 | pmid = 2425357 | pmc = 323864 | doi = 10.1073/pnas.83.13.4962 | doi-access = free | bibcode = 1986PNAS...83.4962K }}
* {{cite journal | vauthors = Scoble HA, Whitaker JN, Biemann K | title = Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry | journal = Journal of Neurochemistry | volume = 47 | issue = 2 | pages = 614–616 | date = August 1986 | pmid = 2426402 | doi = 10.1111/j.1471-4159.1986.tb04544.x | s2cid = 22531833 }}
* {{cite journal | vauthors = Roth HJ, Kronquist K, Pretorius PJ, Crandall BF, Campagnoni AT | title = Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant | journal = Journal of Neuroscience Research | volume = 16 | issue = 1 | pages = 227–238 | year = 1986 | pmid = 2427738 | doi = 10.1002/jnr.490160120 | s2cid = 38277667 }}
* {{cite journal | vauthors = Popko B, Puckett C, Lai E, Shine HD, Readhead C, Takahashi N, Hunt SW, Sidman RL, Hood L | display-authors = 6 | title = Myelin deficient mice: expression of myelin basic protein and generation of mice with varying levels of myelin | journal = Cell | volume = 48 | issue = 4 | pages = 713–721 | date = February 1987 | pmid = 2434243 | doi = 10.1016/0092-8674(87)90249-2 | s2cid = 25224473 }}
* {{cite journal | vauthors = Kamholz J, Spielman R, Gogolin K, Modi W, O'Brien S, Lazzarini R | title = The human myelin-basic-protein gene: chromosomal localization and RFLP analysis | journal = American Journal of Human Genetics | volume = 40 | issue = 4 | pages = 365–373 | date = April 1987 | pmid = 2437795 | pmc = 1684086 }}
* {{cite journal | vauthors = Roth HJ, Kronquist KE, Kerlero de Rosbo N, Crandall BF, Campagnoni AT | title = Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning | journal = Journal of Neuroscience Research | volume = 17 | issue = 4 | pages = 321–328 | year = 1987 | pmid = 2442403 | doi = 10.1002/jnr.490170402 | s2cid = 37138877 }}
* {{cite journal | vauthors = Shoji S, Ohnishi J, Funakoshi T, Fukunaga K, Miyamoto E, Ueki H, Kubota Y | title = Phosphorylation sites of bovine brain myelin basic protein phosphorylated with Ca2+-calmodulin-dependent protein kinase from rat brain | journal = Journal of Biochemistry | volume = 102 | issue = 5 | pages = 1113–1120 | date = November 1987 | pmid = 2449425 | doi = 10.1093/oxfordjournals.jbchem.a122149 | doi-access =  }}
* {{cite journal | vauthors = Wood DD, Moscarello MA | title = The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein | journal = The Journal of Biological Chemistry | volume = 264 | issue = 9 | pages = 5121–5127 | date = March 1989 | pmid = 2466844 | doi = 10.1016/S0021-9258(18)83707-3 | doi-access = free }}
* {{cite journal | vauthors = Edwards AM, Ross NW, Ulmer JB, Braun PE | title = Interaction of myelin basic protein and proteolipid protein | journal = Journal of Neuroscience Research | volume = 22 | issue = 1 | pages = 97–102 | date = January 1989 | pmid = 2467009 | doi = 10.1002/jnr.490220113 | s2cid = 33666906 }}
* {{cite journal | vauthors = Streicher R, Stoffel W | title = The organization of the human myelin basic protein gene. Comparison with the mouse gene | journal = Biological Chemistry Hoppe-Seyler | volume = 370 | issue = 5 | pages = 503–510 | date = May 1989 | pmid = 2472816 | doi = 10.1515/bchm3.1989.370.1.503 }}
* {{cite journal | vauthors = Lennon VA, Wilks AV, Carnegie PR | title = Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin | journal = Journal of Immunology | volume = 105 | issue = 5 | pages = 1223–1230 | date = November 1970 | doi = 10.4049/jimmunol.105.5.1223 | pmid = 4099924 | s2cid = 26451118 | doi-access = free }}
* {{cite journal | vauthors = Carnegie PR | title = Amino acid sequence of the encephalitogenic basic protein from human myelin | journal = The Biochemical Journal | volume = 123 | issue = 1 | pages = 57–67 | date = June 1971 | pmid = 4108501 | pmc = 1176899 | doi = 10.1042/bj1230057 }}
* {{cite journal | vauthors = Baldwin GS, Carnegie PR | title = Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin | journal = Science | volume = 171 | issue = 3971 | pages = 579–581 | date = February 1971 | pmid = 4924231 | doi = 10.1126/science.171.3971.579 | s2cid = 36959912 | bibcode = 1971Sci...171..579B }}
* {{cite journal | vauthors = Baldwin GS, Carnegie PR | title = Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin | journal = The Biochemical Journal | volume = 123 | issue = 1 | pages = 69–74 | date = June 1971 | pmid = 5128665 | pmc = 1176900 | doi = 10.1042/bj1230069 }}
* {{cite journal | vauthors = Wood DD, Vella GJ, Moscarello MA | title = Interaction between human myelin basic protein and lipophilin | journal = Neurochemical Research | volume = 9 | issue = 10 | pages = 1523–1531 | date = October 1984 | pmid = 6083474 | doi = 10.1007/BF00964678 | s2cid = 9751765 }}
* {{cite journal | vauthors = Gibson BW, Gilliom RD, Whitaker JN, Biemann K | title = Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry | journal = The Journal of Biological Chemistry | volume = 259 | issue = 8 | pages = 5028–5031 | date = April 1984 | pmid = 6201481 | doi = 10.1016/S0021-9258(17)42950-4 | doi-access = free }}
* {{cite journal | vauthors = Pribyl TM, Campagnoni CW, Kampf K, Kashima T, Handley VW, McMahon J, Campagnoni AT | title = The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 90 | issue = 22 | pages = 10695–10699 | date = November 1993 | pmid = 7504278 | pmc = 47844 | doi = 10.1073/pnas.90.22.10695 | doi-access = free | bibcode = 1993PNAS...9010695P }}
* {{cite journal  |vauthors=Shanshiashvili L, Mikeladze D |title=Some aspects of myelin basic protein. |journal=J. Biol. Phys. Chem. |volume=3 |issue=3 |pages= 96–9 |year= 2003 |doi=10.4024/18SH03R.jbpc.03.03  }}

{{refend}}

== External links ==
*{{Commons category-inline|Myelin basic proteins}}
* {{PDBe-KB2|P02686|Myelin basic protein}}

{{NLM content}}
{{PDB Gallery|geneid=4155}}
{{Membrane proteins}}

{{DEFAULTSORT:Myelin Basic Protein}}
[[Category:Peripheral membrane proteins]]
[[Category:Human proteins]]
[[Category:Protein families]]