HGNC Approved Gene Symbol:MB
Cytogenetic location:22q12.3 Genomic coordinates(GRCh38) :22:35,606,764-35,623,354 (from NCBI)
The MB gene encodes myoglobin, a cytoplasmic globular hemoprotein highly expressed in skeletal myofibers and cardiac myocytes. Myoglobin binds oxygen (O2) and facilitates its intracellular transport; it plays a role in the control of nitric oxide and reactive oxygen species (ROS) (summary byOlive et al., 2019).
Weller et al. (1984) andAkaboshi (1985) independently cloned human MB, which encodes a protein of 152 residues.
Weller et al. (1984) determined that the MB gene contains 3 exons spanning 10.4 kb.
Jeffreys et al. (1984) used DNA probes isolated from the cloned myoglobin gene to map the gene in human-rodent somatic cell hybrids. The myoglobin locus mapped to chromosome 22q11-q13.Julier et al. (1985) confirmed assignment to chromosome 22.Julier et al. (1985) concluded from multilocus linkage tests that the oncogene SIS locus is most likely distal to MB and that both are distal to IGL. The following tentative map was derived: cen--IGL--0.10--D22S1--0.20--MB--0.07--(SIS, P1).
Two structural variants of myoglobin were described byBoyer et al. (1963).Boulton et al. (1969) studied postmortem muscle from 2,500 persons. Two myoglobin variants were found, and in one of these substitution of lysine for glutamic acid at residue 53 was demonstrated. LaterBoulton et al. (1970) described a variant myoglobin with substitution of glutamine for arginine at residue 139. A third substitution is tryptophan for arginine at residue 139 and a fourth is asparagine for lysine at residue 133 (Romero-Herrera and Lehmann (1971,1974)).
Sarcoplasmic Body Myopathy
In affected members of 6 unrelated families of European descent with sarcoplasmic body myopathy (MYOSB;620286),Olive et al. (2019) identified a heterozygous missense mutation in the MB gene (H98Y;160000.0001). The mutation in the families was found through different methods, including whole-exome sequencing (F1 and F2), linkage analysis and candidate gene sequencing (F3), and direct sequencing of the MB gene (F4, F5, and F6). The mutation was confirmed by Sanger sequencing and segregated with the disorder in all families. It was not present in public databases, including gnomAD. Family F3 had previously been reported byEdstrom et al. (1980). Haplotype analysis did not reveal a founder effect, suggesting that H98Y is a recurrent mutation. Biochemical characterization indicated that the mutant myoglobin has altered O2 binding, exhibits a faster heme dissociation rate, and has a lower reduction potential compared to wildtype. Patient muscle biopsy samples showed evidence of lipid oxidation, increased intracellular superoxide, and increased sulfur content within sarcoplasmic bodies.
In a 75-year-old Asian woman with MYOSB,Hama et al. (2022) identified heterozygosity for the H98Y mutation in the MB gene. The mutation was found by whole-exome sequencing. Functional studies were not performed.
For a DNA sequence that contains tandem repeats but represents only a single locus, White (seeNakamura et al., 1987) introduced the designation variable number of tandem repeats (VNTR) locus. The first polymorphic locus discovered with an arbitrary DNA probe represented such a locus (Wyman and White, 1980; see107750) with fragments of more than 15 different lengths observed in a small sample of unrelated persons. Subsequently, similar systems were observed in several other loci, such as the insulin gene (176730), the Harvey-ras gene (190020), the zeta-globin pseudogene (see142310), the myoglobin gene, and the X-gene region of hepatitis B virus. This region of the HBV genome is thought to be the viral site of integration into the human genome and thus could be considered recombinogenic in a manner similar to the long terminal repeat regions of retroviruses. The repeats in these hypervariable loci have 11 to 60 basepairs. The length of each restriction fragment is a function of the number of copies of the tandem repeat sequence within the fragment. These hypervariable loci are highly informative markers for linkage studies.Jeffreys et al. (1985) found that a DNA probe based on a set of tandem repeats associated with the myoglobin locus can detect by hybridization to human genomic DNA a number of loci containing tandem repeats of similar sequence. The restriction fragment pattern revealed by the sum of the VNTR loci containing such related sequences, scattered through the genome, constitutes a 'fingerprint' unique to the individual.
Garry et al. (1998) created mice without myoglobin by targeted disruption of the myoglobin gene. The mice were fertile and exhibited normal exercise capacity and a normal ventilatory response to hypoxia. Although heart and soleus muscles were depigmented, they functioned normally in standard in vitro assays of muscle performance across a range of work conditions and oxygen availability. These data demonstrated that myoglobin is not essential to meet the metabolic requirements of pregnancy or exercise in a terrestrial mammal, and raise new questions about oxygen transport and metabolic regulation in working muscles. Whether simple diffusion is enough or other mechanisms exist to facilitate high rates of oxygen transport to working myocytes remained to be elucidated.
Godecke et al. (1999) used homologous recombination to delete exon 2 of the mouse Mb gene. They found that Mb -/- mice appeared phenotypically normal but had significantly elevated levels of hemoglobin and an increase in coronary flow and coronary reserve. Histologic analysis demonstrated increased capillary density in the hearts of Mb-deficient mice.Godecke et al. (1999) concluded that disruption of myoglobin results in the activation of multiple compensatory mechanisms that steepen the pO2 gradient to mitochondria, suggesting that myoglobin is important for the delivery of oxygen to mitochondria.
In affected members of 6 unrelated families of European descent with sarcoplasmic body myopathy (MYOSB;620286),Olive et al. (2019) identified a heterozygous c.292C-T transition in the MB gene, resulting in a his98-to-tyr (H98Y) substitution at a highly conserved residue in the proximity of the oxygen-binding heme group. The mutation in the families was found through different methods, including whole-exome sequencing (F1 and F2), linkage analysis and candidate gene sequencing (F3), and direct sequencing of the MB gene (F4, F5, and F6). The mutation was confirmed by Sanger sequencing and segregated with the disorder in all families. It was not present in public databases, including gnomAD. Family F3 had previously been reported byEdstrom et al. (1980).
In a 75-year-old Asian woman with MYOSB,Hama et al. (2022) identified a heterozygous H98Y mutation in the MB gene. The mutation was found by whole-exome sequencing. Functional studies were not performed.
Hofbauer et al. (2022) demonstrated that the mutant H98Y protein showed increased reactivity toward hydrogen peroxide, had a tendency to form aggregates, and was more prone to heme bleaching compared to wildtype. These effects result in impaired oxygen binding capacity and faster heme dissociation compared to wildtype. The biochemical alterations likely play a role in the pathogenesis of the disease.
Akaboshi, E.Cloning of the human myoglobin gene. Gene 33: 241-249, 1985. [PubMed:2989088,related citations] [Full Text]
Boulton, F. E., Huntsman, R. G., Lehmann, H., Lorkin, P. A., Romero-Herrera, A. E.Myoglobin variants. (Abstract) Biochem. J. 118: 39P only, 1970.
Boulton, F. E., Huntsman, R. G., Lorkin, P. A., Lehmann, H.Abnormal human myoglobin: 53(D4) glutamic acid lysine. Nature 223: 832-833, 1969. [PubMed:5805522,related citations] [Full Text]
Boulton, F. E., Huntsman, R. G., Yawson, G. I., Romero-Herrera, A. E., Lorkin, P. A.The second variant of human myoglobin: 138(H16) arginine to glutamine. Brit. J. Haemat. 20A: 69-74, 1971. [PubMed:5540041,related citations] [Full Text]
Boyer, S. H., Fainer, D. C., Naughton, M. A.Myoglobin inherited structural variation in man. Science 140: 1228-1231, 1963. [PubMed:14014717,related citations] [Full Text]
Boyer, S. H.Similar incidence and non-randomness among human myoglobin and hemoglobin mutants in general populations: implications for the study of myoglobin in muscle disease. In: Pathogenesis of Human Muscular Dystrophies. Proceedings of the Vth International Congress of the Muscular Dystrophy Association, Durango, Colo., June 21-25, 1976. Amsterdam: Excerpta Medica (pub.) 1977.
Dozier, C., Walbaum, S., Leprince, D., Stehelin, D.EcoRI RFLP linked to the human myb gene. Nucleic Acids Res. 14: 1928 only, 1986. [PubMed:3005993,related citations] [Full Text]
Edstrom, L., Thornell, L.-E., Eriksson, A.A new type of hereditary distal myopathy with characteristic sarcoplasmic bodies and intermediate (skeletin) filaments. J. Neurol. Sci. 47: 171-190, 1980. [PubMed:6251174,related citations] [Full Text]
Garry, D. J., Ordway, G. A., Lorenz, J. N., Radford, N. B., Chin, E. R., Grange, R. W., Bassel-Duby, R., Williams, R. S.Mice without myoglobin. Nature 395: 905-908, 1998. [PubMed:9804424,related citations] [Full Text]
Godecke, A., Flogel, U., Zanger, K., Ding, Z., Hirchenhain, J., Decking, U. K. M., Schrader, J.Disruption of myoglobin in mice induces multiple compensatory mechanisms. Proc. Nat. Acad. Sci. 96: 10495-10500, 1999. [PubMed:10468637,images,related citations] [Full Text]
Hama, Y., Mori-Yoshimura, M., Aizawa, K., Oya, Y., Nakamura, H., Inoue, M., Iida, A., Sato, N., Nonaka, I., Nishino, I., Takahashi, Y.Myoglobinopathy affecting facial and oropharyngeal muscles. Neuromusc. Disord. 32: 516-520, 2022. [PubMed:35527200,related citations] [Full Text]
Hofbauer, S., Pignataro, M., Borsari, M., Bortolotti, C. A., Di Rocco, G., Ravenscroft, G., Furtmuller, P. G., Obinger, C., Sola, M., Battistuzzi, G.Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy. FEBS J. 289: 1105-1117, 2022. [PubMed:34679218,images,related citations] [Full Text]
Jeffreys, A. J., Wilson, V., Blanchetot, A., Weller, P., Geurts van Kessel, A., Spurr, N., Solomon, E., Goodfellow, P.The human myoglobin gene: a third dispersed globin locus in the human genome. Nucleic Acids Res. 12: 3235-3243, 1984. [PubMed:6326055,related citations] [Full Text]
Jeffreys, A., Wilson, V., Thein, S.Hypervariable 'minisatellite' regions in human DNA. Nature 314: 67-73, 1985. [PubMed:3856104,related citations] [Full Text]
Julier, C., Lathrop, M., Lalouel, J. M., Kaplan, J. C.Use of multilocus tests of gene order: example for chromosome 22. (Abstract) Cytogenet. Cell Genet. 40: 663-664, 1985.
Julier, C., Lathrop, M., Lalouel, J. M., Reghis, A., Szajnert, M. F., Kaplan, J. C.New restriction fragment length polymorphisms on human chromosome 22 at loci SIS, MB and IGLV. (Abstract) Cytogenet. Cell Genet. 40: 664 only, 1985.
Julier, C., Reghis, A., Szajnert, M. F., Kaplan, J. C., Lathrop, G. M., Lalouel, J. M.A preliminary linkage map of human chromosome 22. (Abstract) Cytogenet. Cell Genet. 40: 665 only, 1985.
Nakamura, Y., Leppert, M., O'Connell, P., Wolff, R., Holm, T., Culver, M., Martin, C., Fujimoto, E., Hoff, M., Kumlin, E., White, R.Variable number of tandem repeat (VNTR) markers for human gene mapping. Science 235: 1616-1622, 1987. [PubMed:3029872,related citations] [Full Text]
Olive, M., Engvall, M., Ravenscroft, G., Cabrera-Serrano, M., Jiao, H., Bortolotti, C. A., Pignataro, M., Lambrughi, M., Jiang, H., Forrest, A. R. R., Benseny-Cases, N., Hofbauer, S., and 32 others.Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions. Nature Commun. 10: 1396, 2019. [PubMed:30918256,images,related citations] [Full Text]
Romero-Herrera, A. E., Lehmann, H.Primary structure of human myoglobin. Nature N.B. 232: 149-152, 1971. [PubMed:5285572,related citations] [Full Text]
Romero-Herrera, A. E., Lehmann, H.The amino acid sequence of human myoglobin and its minor fractions. Proc. Roy. Soc. London 186B: 249-279, 1974. [PubMed:4153103,related citations] [Full Text]
Weller, P., Jeffreys, A. J., Wilson, V., Blanchetot, A.Organization of the human myoglobin gene. EMBO J. 3: 439-446, 1984. [PubMed:6571704,related citations] [Full Text]
Wyman, A. R., White, R.A highly polymorphic locus in human DNA. Proc. Nat. Acad. Sci. 77: 6754-6758, 1980. [PubMed:6935681,related citations] [Full Text]
HGNC Approved Gene Symbol: MB
Cytogenetic location: 22q12.3 Genomic coordinates(GRCh38) : 22:35,606,764-35,623,354(from NCBI)
| Location | Phenotype | Phenotype MIM number | Inheritance | Phenotype mapping key |
|---|---|---|---|---|
| 22q12.3 | Myopathy, sarcoplasmic body | 620286 | Autosomal dominant | 3 |
The MB gene encodes myoglobin, a cytoplasmic globular hemoprotein highly expressed in skeletal myofibers and cardiac myocytes. Myoglobin binds oxygen (O2) and facilitates its intracellular transport; it plays a role in the control of nitric oxide and reactive oxygen species (ROS) (summary by Olive et al., 2019).
Weller et al. (1984) and Akaboshi (1985) independently cloned human MB, which encodes a protein of 152 residues.
Weller et al. (1984) determined that the MB gene contains 3 exons spanning 10.4 kb.
Jeffreys et al. (1984) used DNA probes isolated from the cloned myoglobin gene to map the gene in human-rodent somatic cell hybrids. The myoglobin locus mapped to chromosome 22q11-q13. Julier et al. (1985) confirmed assignment to chromosome 22. Julier et al. (1985) concluded from multilocus linkage tests that the oncogene SIS locus is most likely distal to MB and that both are distal to IGL. The following tentative map was derived: cen--IGL--0.10--D22S1--0.20--MB--0.07--(SIS, P1).
Two structural variants of myoglobin were described by Boyer et al. (1963). Boulton et al. (1969) studied postmortem muscle from 2,500 persons. Two myoglobin variants were found, and in one of these substitution of lysine for glutamic acid at residue 53 was demonstrated. Later Boulton et al. (1970) described a variant myoglobin with substitution of glutamine for arginine at residue 139. A third substitution is tryptophan for arginine at residue 139 and a fourth is asparagine for lysine at residue 133 (Romero-Herrera and Lehmann (1971, 1974)).
Sarcoplasmic Body Myopathy
In affected members of 6 unrelated families of European descent with sarcoplasmic body myopathy (MYOSB; 620286), Olive et al. (2019) identified a heterozygous missense mutation in the MB gene (H98Y; 160000.0001). The mutation in the families was found through different methods, including whole-exome sequencing (F1 and F2), linkage analysis and candidate gene sequencing (F3), and direct sequencing of the MB gene (F4, F5, and F6). The mutation was confirmed by Sanger sequencing and segregated with the disorder in all families. It was not present in public databases, including gnomAD. Family F3 had previously been reported by Edstrom et al. (1980). Haplotype analysis did not reveal a founder effect, suggesting that H98Y is a recurrent mutation. Biochemical characterization indicated that the mutant myoglobin has altered O2 binding, exhibits a faster heme dissociation rate, and has a lower reduction potential compared to wildtype. Patient muscle biopsy samples showed evidence of lipid oxidation, increased intracellular superoxide, and increased sulfur content within sarcoplasmic bodies.
In a 75-year-old Asian woman with MYOSB, Hama et al. (2022) identified heterozygosity for the H98Y mutation in the MB gene. The mutation was found by whole-exome sequencing. Functional studies were not performed.
For a DNA sequence that contains tandem repeats but represents only a single locus, White (see Nakamura et al., 1987) introduced the designation variable number of tandem repeats (VNTR) locus. The first polymorphic locus discovered with an arbitrary DNA probe represented such a locus (Wyman and White, 1980; see 107750) with fragments of more than 15 different lengths observed in a small sample of unrelated persons. Subsequently, similar systems were observed in several other loci, such as the insulin gene (176730), the Harvey-ras gene (190020), the zeta-globin pseudogene (see 142310), the myoglobin gene, and the X-gene region of hepatitis B virus. This region of the HBV genome is thought to be the viral site of integration into the human genome and thus could be considered recombinogenic in a manner similar to the long terminal repeat regions of retroviruses. The repeats in these hypervariable loci have 11 to 60 basepairs. The length of each restriction fragment is a function of the number of copies of the tandem repeat sequence within the fragment. These hypervariable loci are highly informative markers for linkage studies. Jeffreys et al. (1985) found that a DNA probe based on a set of tandem repeats associated with the myoglobin locus can detect by hybridization to human genomic DNA a number of loci containing tandem repeats of similar sequence. The restriction fragment pattern revealed by the sum of the VNTR loci containing such related sequences, scattered through the genome, constitutes a 'fingerprint' unique to the individual.
Garry et al. (1998) created mice without myoglobin by targeted disruption of the myoglobin gene. The mice were fertile and exhibited normal exercise capacity and a normal ventilatory response to hypoxia. Although heart and soleus muscles were depigmented, they functioned normally in standard in vitro assays of muscle performance across a range of work conditions and oxygen availability. These data demonstrated that myoglobin is not essential to meet the metabolic requirements of pregnancy or exercise in a terrestrial mammal, and raise new questions about oxygen transport and metabolic regulation in working muscles. Whether simple diffusion is enough or other mechanisms exist to facilitate high rates of oxygen transport to working myocytes remained to be elucidated.
Godecke et al. (1999) used homologous recombination to delete exon 2 of the mouse Mb gene. They found that Mb -/- mice appeared phenotypically normal but had significantly elevated levels of hemoglobin and an increase in coronary flow and coronary reserve. Histologic analysis demonstrated increased capillary density in the hearts of Mb-deficient mice. Godecke et al. (1999) concluded that disruption of myoglobin results in the activation of multiple compensatory mechanisms that steepen the pO2 gradient to mitochondria, suggesting that myoglobin is important for the delivery of oxygen to mitochondria.
In affected members of 6 unrelated families of European descent with sarcoplasmic body myopathy (MYOSB; 620286), Olive et al. (2019) identified a heterozygous c.292C-T transition in the MB gene, resulting in a his98-to-tyr (H98Y) substitution at a highly conserved residue in the proximity of the oxygen-binding heme group. The mutation in the families was found through different methods, including whole-exome sequencing (F1 and F2), linkage analysis and candidate gene sequencing (F3), and direct sequencing of the MB gene (F4, F5, and F6). The mutation was confirmed by Sanger sequencing and segregated with the disorder in all families. It was not present in public databases, including gnomAD. Family F3 had previously been reported by Edstrom et al. (1980).
In a 75-year-old Asian woman with MYOSB, Hama et al. (2022) identified a heterozygous H98Y mutation in the MB gene. The mutation was found by whole-exome sequencing. Functional studies were not performed.
Hofbauer et al. (2022) demonstrated that the mutant H98Y protein showed increased reactivity toward hydrogen peroxide, had a tendency to form aggregates, and was more prone to heme bleaching compared to wildtype. These effects result in impaired oxygen binding capacity and faster heme dissociation compared to wildtype. The biochemical alterations likely play a role in the pathogenesis of the disease.
Akaboshi, E.Cloning of the human myoglobin gene. Gene 33: 241-249, 1985. [PubMed: 2989088] [Full Text: https://doi.org/10.1016/0378-1119(85)90231-8]
Boulton, F. E., Huntsman, R. G., Lehmann, H., Lorkin, P. A., Romero-Herrera, A. E.Myoglobin variants. (Abstract) Biochem. J. 118: 39P only, 1970.
Boulton, F. E., Huntsman, R. G., Lorkin, P. A., Lehmann, H.Abnormal human myoglobin: 53(D4) glutamic acid lysine. Nature 223: 832-833, 1969. [PubMed: 5805522] [Full Text: https://doi.org/10.1038/223832a0]
Boulton, F. E., Huntsman, R. G., Yawson, G. I., Romero-Herrera, A. E., Lorkin, P. A.The second variant of human myoglobin: 138(H16) arginine to glutamine. Brit. J. Haemat. 20A: 69-74, 1971. [PubMed: 5540041] [Full Text: https://doi.org/10.1111/j.1365-2141.1971.tb00787.x]
Boyer, S. H., Fainer, D. C., Naughton, M. A.Myoglobin inherited structural variation in man. Science 140: 1228-1231, 1963. [PubMed: 14014717] [Full Text: https://doi.org/10.1126/science.140.3572.1228-a]
Boyer, S. H.Similar incidence and non-randomness among human myoglobin and hemoglobin mutants in general populations: implications for the study of myoglobin in muscle disease. In: Pathogenesis of Human Muscular Dystrophies. Proceedings of the Vth International Congress of the Muscular Dystrophy Association, Durango, Colo., June 21-25, 1976. Amsterdam: Excerpta Medica (pub.) 1977.
Dozier, C., Walbaum, S., Leprince, D., Stehelin, D.EcoRI RFLP linked to the human myb gene. Nucleic Acids Res. 14: 1928 only, 1986. [PubMed: 3005993] [Full Text: https://doi.org/10.1093/nar/14.4.1928]
Edstrom, L., Thornell, L.-E., Eriksson, A.A new type of hereditary distal myopathy with characteristic sarcoplasmic bodies and intermediate (skeletin) filaments. J. Neurol. Sci. 47: 171-190, 1980. [PubMed: 6251174] [Full Text: https://doi.org/10.1016/0022-510x(80)90002-7]
Garry, D. J., Ordway, G. A., Lorenz, J. N., Radford, N. B., Chin, E. R., Grange, R. W., Bassel-Duby, R., Williams, R. S.Mice without myoglobin. Nature 395: 905-908, 1998. [PubMed: 9804424] [Full Text: https://doi.org/10.1038/27681]
Godecke, A., Flogel, U., Zanger, K., Ding, Z., Hirchenhain, J., Decking, U. K. M., Schrader, J.Disruption of myoglobin in mice induces multiple compensatory mechanisms. Proc. Nat. Acad. Sci. 96: 10495-10500, 1999. [PubMed: 10468637] [Full Text: https://doi.org/10.1073/pnas.96.18.10495]
Hama, Y., Mori-Yoshimura, M., Aizawa, K., Oya, Y., Nakamura, H., Inoue, M., Iida, A., Sato, N., Nonaka, I., Nishino, I., Takahashi, Y.Myoglobinopathy affecting facial and oropharyngeal muscles. Neuromusc. Disord. 32: 516-520, 2022. [PubMed: 35527200] [Full Text: https://doi.org/10.1016/j.nmd.2022.02.010]
Hofbauer, S., Pignataro, M., Borsari, M., Bortolotti, C. A., Di Rocco, G., Ravenscroft, G., Furtmuller, P. G., Obinger, C., Sola, M., Battistuzzi, G.Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy. FEBS J. 289: 1105-1117, 2022. [PubMed: 34679218] [Full Text: https://doi.org/10.1111/febs.16235]
Jeffreys, A. J., Wilson, V., Blanchetot, A., Weller, P., Geurts van Kessel, A., Spurr, N., Solomon, E., Goodfellow, P.The human myoglobin gene: a third dispersed globin locus in the human genome. Nucleic Acids Res. 12: 3235-3243, 1984. [PubMed: 6326055] [Full Text: https://doi.org/10.1093/nar/12.7.3235]
Jeffreys, A., Wilson, V., Thein, S.Hypervariable 'minisatellite' regions in human DNA. Nature 314: 67-73, 1985. [PubMed: 3856104] [Full Text: https://doi.org/10.1038/314067a0]
Julier, C., Lathrop, M., Lalouel, J. M., Kaplan, J. C.Use of multilocus tests of gene order: example for chromosome 22. (Abstract) Cytogenet. Cell Genet. 40: 663-664, 1985.
Julier, C., Lathrop, M., Lalouel, J. M., Reghis, A., Szajnert, M. F., Kaplan, J. C.New restriction fragment length polymorphisms on human chromosome 22 at loci SIS, MB and IGLV. (Abstract) Cytogenet. Cell Genet. 40: 664 only, 1985.
Julier, C., Reghis, A., Szajnert, M. F., Kaplan, J. C., Lathrop, G. M., Lalouel, J. M.A preliminary linkage map of human chromosome 22. (Abstract) Cytogenet. Cell Genet. 40: 665 only, 1985.
Nakamura, Y., Leppert, M., O'Connell, P., Wolff, R., Holm, T., Culver, M., Martin, C., Fujimoto, E., Hoff, M., Kumlin, E., White, R.Variable number of tandem repeat (VNTR) markers for human gene mapping. Science 235: 1616-1622, 1987. [PubMed: 3029872] [Full Text: https://doi.org/10.1126/science.3029872]
Olive, M., Engvall, M., Ravenscroft, G., Cabrera-Serrano, M., Jiao, H., Bortolotti, C. A., Pignataro, M., Lambrughi, M., Jiang, H., Forrest, A. R. R., Benseny-Cases, N., Hofbauer, S., and 32 others.Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions. Nature Commun. 10: 1396, 2019. [PubMed: 30918256] [Full Text: https://doi.org/10.1038/s41467-019-09111-2]
Romero-Herrera, A. E., Lehmann, H.Primary structure of human myoglobin. Nature N.B. 232: 149-152, 1971. [PubMed: 5285572] [Full Text: https://doi.org/10.1038/newbio232149a0]
Romero-Herrera, A. E., Lehmann, H.The amino acid sequence of human myoglobin and its minor fractions. Proc. Roy. Soc. London 186B: 249-279, 1974. [PubMed: 4153103] [Full Text: https://doi.org/10.1098/rspb.1974.0048]
Weller, P., Jeffreys, A. J., Wilson, V., Blanchetot, A.Organization of the human myoglobin gene. EMBO J. 3: 439-446, 1984. [PubMed: 6571704] [Full Text: https://doi.org/10.1002/j.1460-2075.1984.tb01825.x]
Wyman, A. R., White, R.A highly polymorphic locus in human DNA. Proc. Nat. Acad. Sci. 77: 6754-6758, 1980. [PubMed: 6935681] [Full Text: https://doi.org/10.1073/pnas.77.11.6754]
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