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. 2023 Aug 26;50:109520. doi: 10.1016/j.dib.2023.109520

Table 1.

Citations for the 269 studies that met the selection criteria and were included in the meta-analysis.

Number Citation
1 Acevedo, L.M., Rivero, J.L.L., 2006. New insights into skeletal muscle fibre types in the dog with particular focus towards hybrid myosin phenotypes. Cell Tissue Res 323, 283–303. https://doi.org/10.1007/s00441-005-0057-4
2 Acosta, L., Roy, R.R., 1987. Fiber-type composition of selected hindlimb muscles of a primate (cynomolgus monkey). Anat Rec 218, 136–141. https://doi.org/10.1002/ar.1092180207
3 Agostini, de Martino, L., Soltau, B., Hasselbach, W., 1991. The Modulation of the Calcium Transport by Skeletal Muscle Sarcoplasmic Reticulum in the Hibernating European Hamster. Zeitschrift für Naturforschung C 46, 1109–1126. https://doi.org/10.1515/znc-1991-11-1229
4 Aigner, S., Gohlsch, B., Hämaläinen, N., Staron, R.S., Uber, A., Wehrle, U., Pette, D., 1993. Fast myosin heavy chain diversity in skeletal muscles of the rabbit: heavy chain IId, not IIb predominates. Eur J Biochem 211, 367–372. https://doi.org/10.1111/j.1432-1033.1993.tb19906.x
5 Almeida-Silveira, M.I., Pérot, C., Pousson, M., Goubel, F., 1994. Effects of stretch-shortening cycle training on mechanical properties and fibre type transition in the rat soleus muscle. Pflug Arch Eur J Physiol 427, 289–94. https://doi.org/10.1007/BF00374536
6 Alnaqeeb, M.A., Al-Baker, E., 1994. Muscle fiber type, number and size in the EDL and soleus of Jaculus jaculus. J. Univ. Kuwait (Sci.) 21, 231–241.
7 Alvarez, G.I., Díaz, A.O., Longo, M. v., Becerra, F., Vassallo, A.I., 2012. Histochemical and Morphometric Analyses of the Musculature of the Forelimb of the Subterranean Rodent Ctenomys talarum (Octodontoidea). J Vet Med C: Anat Histol Embryol41, 317–325. https://doi.org/10.1111/j.1439-0264.2012.01137.x
8 Anapol, F.C., Jungers, W.L., 1986. Architectural and histochemical diversity within the quadriceps femoris of the brown lemur (Lemur fulvus). Am J Phys Anthropol 69, 355–375. https://doi.org/10.1002/ajpa.1330690308
9 Ansved, T., 1995. Effects of immobilization on the rat soleus muscle in relation to age. Acta Physiol Scand 154, 291–302. https://doi.org/10.1111/j.1748-1716.1995.tb09913.x
10 Arbanas, J., Klasan, G.S., Nikolić, M., Cvijanović, O., Malnar, D., 2010. Immunohistochemical analysis of the human psoas major muscle with regards to the body side and aging. Coll Antropol 34 Suppl 2, 169–73.
11 Arbanas, J., Klasan, G.S., Nikolic, M., Jerkovic, R., Miljanovic, I., Malnar, D., 2009. Fibre type composition of the human psoas major muscle with regard to the level of its origin. J Anat 215, 636–41. https://doi.org/10.1111/j.1469-7580.2009.01155.x
12 Ariano, M.A., Edgerton, V.R., Armstrong, R.B., 1973. Hindlimb muscle fiber populations of five mammals. J Histochem Cytochem 21, 51–55. https://doi.org/10.1177/21.1.51
13 Armstrong, R.B., Ianuzzo, C.D., Kunz, T.H., 1977. Histochemical and biochemical properties of flight muscle fibers in the little brown bat,Myotis lucifugus. J Comp Physiol B: Biochem Syst Environ Physiol 119, 141–154. https://doi.org/10.1007/BF00686562
14 Armstrong, R.B., Phelps, R.O., 1984. Muscle fiber type composition of the rat hindlimb. Am J Anat 171, 259–272. https://doi.org/10.1002/aja.1001710303
15 Armstrong, R.B., Saubert, C.W., Seeherman, H.J., Taylor, C.R., 1982. Distribution of fiber types in locomotory muscles of dogs. Am J Anat 163, 87–98. https://doi.org/10.1002/aja.1001630107
16 Asmussen, G., Gaunitz, U., 1989. Temperature effects on isometric contractions of slow and fast twitch muscles of various rodents–dependence on fibre type composition: a comparative study. Biomed Biochim Acta 48, S536-41.
17 Augusto, V., Padovani, C.R., Rocha Campos, G.E., 2004. Skeletal muscle fiber types in C57Bl6J mice. Braz J Morphol Sci 21, 89–94.
18 Bao, T., Han, H., Li, B., Zhao, Y., Bou, G., Zhang, X., Du, M., Zhao, R., Mongke, T., Laxima, Ding, W., Jia, Z., Dugarjaviin, M., Bai, D., 2020. The distinct transcriptomes of fast-twitch and slow-twitch muscles in Mongolian horses. Comp Biochem Physiol Part D Genomics Proteomics 33, 100649. https://doi.org/10.1016/j.cbd.2019.100649
19 Bär, A., Pette, D., 1988. Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett 235, 153–155. https://doi.org/10.1016/0014-5793(88)81253-5
20 Beecher, G.R., Cassens, R.G., Hoekstra, W.G., Briskey, E.J., 1965. Red and White Fiber Content and Associated Post-Mortem Properties of Seven Porcine Muscles. J Food Sci 30, 969–976. https://doi.org/10.1111/j.1365-2621.1965.tb01872.x
21 Bello, M.A., Roy, R.R., Martin, T.P., Goforth, H.W., Edgerton, V.R., 1985. Axial musculature in the dolphin (Tursiops truncatus): Some architectural and histochemical characteristics. Mar Mamm Sci 1, 324–336. https://doi.org/10.1111/j.1748-7692.1985.tb00019.x
22 Bloemberg, D., Quadrilatero, J., 2012. Rapid determination of myosin heavy chain expression in rat, mouse, and human skeletal muscle using multicolor immunofluorescence analysis. PLoS One 7. https://doi.org/10.1371/journal.pone.0035273
23 Bonington, A., Whitmore, I., Mahon, M., 1987. A histological and histochemical study of the cricopharyngeus muscle in the guinea-pig. J Anat 153, 151–61.
24 Boyd-Clark, L.C., Briggs, C.A., Galea, M.P., 2001. Comparative histochemical composition of muscle fibres in a pre- and a postvertebral muscle of the cervical spine. J Anat 199, 709–716. https://doi.org/10.1017/S0021878201008706
25 Brandstetter, A.M., Picard, B., Geay, Y., 1998. Muscle fibre characteristics in four muscles of growing bulls I. Postnatal differentiation, Livest Prod Sci.
26 Brasseur, J.E., Curtis, R.L., Mellender, J.W., Rimm, A.A., Melvin, J.L., Sulaiman, A.R., 1987. Systematic distribution of muscle fiber types in the medical gastrocnemius of the laboratory mouse: A morphometric analysis. Anat Rec 218, 396–401. https://doi.org/10.1002/ar.1092180407
27 Braund, K.G., Amling, K.A., Mehta, J.R., Steiss, J.E., Scholz, C., 1995. Histochemical and morphometric study of fiber types in ten skeletal muscles of healthy young adult cats. Am J Vet Res 56, 349–57.
28 Braund, K.G., Mcguire, J.A., Lincoln, C.E., 1982. Observations on Normal Skeletal Muscle of Mature Dogs: A Cytochemical, Histochemical, and Morphometric Study, Vet Pathol.
29 Brigham, R.M., Ianuzzo, C.D., Hamilton, N., Fenton, M.B., 1990. Histochemical and biochemical plasticity of muscle fibers in the little brown bat (Myotis lucifugus). J Comp Physiol B: Biochem Syst Environ Physiol 160, 183–186. https://doi.org/10.1007/BF00300951
30 Burke, R.E., 1967. Motor unit types of cat triceps surae muscle. J Physiol 193, 141–160. https://doi.org/10.1113/jphysiol.1967.sp008348
31 Burke, R.E., Levine, D.N., Salcman, M., Tsairis, P., 1974. Motor units in cat soleus muscle: physiological, histochemical and morphological characteristics. J Physiol 238, 503–514. https://doi.org/10.1113/jphysiol.1974.sp010540
32 Burke, R.E., Levine, D.N., Tsairis, P., Zajac, F.E., 1973. Physiological types and histochemical profiles in motor units of the cat gastrocnemius. J Physiol 234, 723–748. https://doi.org/10.1113/jphysiol.1973.sp010369
33 Burkholder, T.J., Fingado, B., Baron, S., Lieber, R.L., 1994. Relationship between muscle fiber types and sizes and muscle architectural properties in the mouse hindlimb. J Morphol 221, 177–190. https://doi.org/10.1002/jmor.1052210207
34 Carlson, H., 1978. Histochemical fiber composition of lumbar back muscles in the cat. Acta Physiol Scand 103, 198–209. https://doi.org/10.1111/j.1748-1716.1978.tb06207.x
35 Casinos, A., Milne, N., Jouffroy, F.K., Médina, M.F., 2016. Muscle fibre types in the reduced forelimb and enlarged hindlimb of the quokka (Setonix brachyurus, Macropodidae). Aust J Zool 64, 277–284. https://doi.org/10.1071/ZO15055
36 Cebesoy, S., 2009. Morphology and histochemistry of primary flight muscles in Rhinolophus mehelyii. Afr J Biotechnol 8, 1160–1164.
37 Cebesoy, S., Ayvali, C., 2003. Morphology and histochemistry of primary flight muscles in Myotis myotis 16, 245–252.
38 Chanaud, C.M., Pratt, C.A., Loeb, G.E., 1991. Functionally complex muscles of the cat hindlimb. Exp Brain Res 85, 300–313. https://doi.org/10.1007/BF00229408
39 Chang, H., Jiang, S., Ma, X., Peng, X., Zhang, J., Wang, Z., Xu, S., Wang, H., Gao, Y., 2018. Proteomic analysis reveals the distinct energy and protein metabolism characteristics involved in myofiber type conversion and resistance of atrophy in the extensor digitorum longus muscle of hibernating Daurian ground squirrels. Comp Biochem Physiol Part D Genomics Proteomics 26, 20–31. https://doi.org/10.1016/j.cbd.2018.02.002
40 Choi, H., Selpides, P.-J.I., Nowell, M.M., Rourke, B.C., 2009. Functional overload in ground squirrel plantaris muscle fails to induce myosin isoform shifts. Am J Physiol Regul Integr Comp Physiol 297, R578-86. https://doi.org/10.1152/ajpregu.00236.2009
41 Chopard, A., Pons, F., Marini, J.F., 2001. Cytoskeletal protein contents before and after hindlimb suspension in a fast and slow rat skeletal muscle. Am J Physiol Regul Integr Comp Physiol 280, R323-30. https://doi.org/10.1152/ajpregu.2001.280.2.R323
42 Collatos, T.C., Edgerton, V.R., Smith, J.L., Botterman, B.R., 1977. Contractile properties and fiber type compositions of flexors and extensors of elbow joint in cat: implications for motor control. J Neurophysiol 40, 1292–1300. https://doi.org/10.1152/jn.1977.40.6.1292
43 Cordonnier, C., Stevens, L., Picquet, F., Mounier, Y., 1995. Structure-function relationship of soleus muscle fibres from the rhesus monkey. Pflug Arch Eur J Physiol 430, 19–25. https://doi.org/10.1007/BF00373835
44 Cornachione, A.S., Benedini-Elias, P.C.O., Polizello, J.C., Carvalho, L.C., Mattiello-Sverzut, A.C., 2011. Characterization of fiber types in different muscles of the hindlimb in female weanling and adult wistar rats. Acta Histochem Cytochem 44, 43–50. https://doi.org/10.1267/ahc.10031
45 Cotton, C.J., Harlow, H.J., 2010. Avoidance of Skeletal Muscle Atrophy in Spontaneous and Facultative Hibernators. Physiol Biochem Zool 83, 551–560. https://doi.org/10.1086/650471
46 Curry, J.W., Hohl, R., Noakes, T.D., Kohn, T.A., 2012. High oxidative capacity and type IIx fibre content in springbok and fallow deer skeletal muscle suggest fast sprinters with a resistance to fatigue. J Exp Biol 215, 3997–4005. https://doi.org/10.1242/jeb.073684
47 Dada, S., Henning, F., Feldmann, D.C., Kohn, T.A., 2018. Baboon (Papio ursinus) single fibre contractile properties are similar to that of trained humans. J Muscle Res Cell Motil 39, 189–199. https://doi.org/10.1007/s10974-019-09509-x
48 de A. Braga, S., G. F. Padilha, F., M. R. Ferreira, A., 2016. Evaluation of Muscle Fiber Types in German Shepherd Dogs of Different Ages. Anat Rec 299, 1540–1547. https://doi.org/10.1002/ar.23464
49 de Diego, M., Casado, A., Gómez, M., Martín, J., Pastor, J.F., Potau, J.M., 2020. Structural and molecular analysis of elbow flexor muscles in modern humans and common chimpanzees. Zoomorphology 139, 277–290. https://doi.org/10.1007/s00435-020-00482-5
50 Delp, M.D., Duan, C., 1996. Composition and size of type I, IIA, IID/X, and IIB fibers and citrate synthase activity of rat muscle. J Appl Physiol 80, 261–270. https://doi.org/10.1152/jappl.1996.80.1.261
51 Dennington, S., Baldwin, J., 1988. Biochemical Correlates of Energy-Metabolism in Muscles Used to Power Hopping by Kangaroos. Aust J Zool 36, 229. https://doi.org/10.1071/ZO9880229
52 Donselaar, Y., Eerbeek, O., Kernell, D., Verhey, B.A., 1987. Fibre sizes and histochemical staining characteristics in normal and chronically stimulated fast muscle of cat. J Physiol 382, 237–54. https://doi.org/10.1113/jphysiol.1987.sp016365
53 Edgerton, V.R., Barnard, R.J., Peter, J.B., Maier, A., Simpson, D.R., 1975a. Properties of immobilized hind-limb muscles of the Galago senegalensis. Exp Neurol 46, 115–131. https://doi.org/10.1016/0014-4886(75)90036-9
54 Edgerton, V.R., Smith, J.L., Simpson, D.R., 1975b. Muscle fibre type populations of human leg muscles. Histochem J 7, 259–266. https://doi.org/10.1007/BF01003594
55 Edström, L., Lindquist, C., 1973. Histochemical fiber composition of some facial muscles in the cat in relation to their contraction properties. Acta Physiol Scand 89, 491–503. https://doi.org/10.1111/j.1748-1716.1973.tb05543.x
56 Edström, L., Nyström, B., 1969. Histochemical types and sizes of fibres in normal human muscles. A biopsy study. Acta Neurol Scand 45, 257–69. https://doi.org/10.1111/j.1600-0404.1969.tb01238.x
57 Egginton, S., 1990. Numerical and areal density estimates of fibre type composition in a skeletal muscle (rat extensor digitorum longus). J Anat 168, 73–80.
58 Eizema, K., van den Burg, M., Kiri, A., Dingboom, E.G., van Oudheusden, H., Goldspink, G., Weijs, W.A., 2003. Differential expression of equine myosin heavy-chain mRNA and protein isoforms in a limb muscle. J Histochem Cytochem 51, 1207–16. https://doi.org/10.1177/002215540305100911
59 Eizema, K., van den Burg, M.M.M., de Jonge, H.W., Dingboom, E.G., Weijs, W.A., Everts, M.E., 2005. Myosin heavy chain isoforms in equine gluteus medius muscle: comparison of mRNA and protein expression profiles. J Histochem Cytochem 53, 1383–90. https://doi.org/10.1369/jhc.4A6609.2005
60 Eng, C.M., Smallwood, L.H., Rainiero, M.P., Lahey, M., Ward, S.R., Lieber, R.L., 2008. Scaling of muscle architecture and fiber types in the rat hindlimb. J Exp Biol 211, 2336–2345. https://doi.org/10.1242/jeb.017640
61 English, A.W., Letbetter, W.D., 1982. A histochemical analysis of identified compartments of cat lateral gastrocnemius muscle. Anat Rec 204, 123–30. https://doi.org/10.1002/ar.1092040205
62 Enríquez, V., Granados, S., Arias, M.P., Calderón, J.C., 2015. Muscle Fiber Types of Gluteus Medius in the Colombian Creole Horse. J Equine Vet Sci 35, 524–530. https://doi.org/10.1016/j.jevs.2015.02.010
63 Essén-Gustavsson, B., Fjelkner-Modig, S., 1985. Skeletal muscle characteristics in different breeds of pigs in relation to sensory properties of meat. Meat Sci 13, 33–47. https://doi.org/10.1016/S0309-1740(85)80003-6
64 Essén-Gustavsson, B., Rehbinder, C., 1985. Skeletal muscle characteristics of reindeer (Rangifer tarandus L.). Comp Biochem Physiol A Physiol 82, 675–679. https://doi.org/10.1016/0300-9629(85)90450-5
65 Feng, X., Zhang, T., Xu, Z., Choi, S.J., Qian, J., Furdui, C.M., Register, T.C., Delbono, O., 2012. Myosin heavy chain isoform expression in the Vastus Lateralis muscle of aging African green vervet monkeys. Exp Gerontol 47, 601–607. https://doi.org/10.1016/j.exger.2012.05.007
66 Fitts, R.H., Bodine, S.C., Romatowski, J.G., Widrick, J.J., 1998. Velocity, force, power, and Ca2+ sensitivity of fast and slow monkey skeletal muscle fibers. J Appl Physiol 84, 1776–87. https://doi.org/10.1152/jappl.1998.84.5.1776
67 Foehring, R.C., Hermanson, J.W., 1984. Morphology and Histochemistry of Flight Muscles in Free-Tailed Bats, Tadarida brasiliensis. J Mammal 65, 388–394. https://doi.org/10.2307/1381084
68 Ford, D.M., Bagnall, K.M., McFadden, K.D., Reid, D.C., 1986. A Comparison of Muscle Fiber Characteristics at Different Levels of the Vertebral Column in the Rhesus Monkey. Cells Tissues Organs 126, 163–166. https://doi.org/10.1159/000146208
69 Francisco, C.L., Jorge, A.M., Dal-Pai-Silva, M., Carani, F.R., Cabeço, L.C., Silva, S.R., 2011. Muscle fiber type characterization and myosin heavy chain (MyHC) isoform expression in Mediterranean buffaloes. Meat Sci 88, 535–541. https://doi.org/10.1016/j.meatsci.2011.02.007
70 Fuentes, I., Cobos, A.R., Segade, L.A.G., 1998. Muscle fibre types and their distribution in the biceps and triceps brachii of the rat and rabbit. J Anat 192, 203–210. https://doi.org/10.1046/j.1469-7580.1998.19220203.x
71 Gao, Y.F., Wang, J., Wang, H.P., Feng, B., Dang, K., Wang, Q., Hinghofer-Szalkay, H.G., 2012. Skeletal muscle is protected from disuse in hibernating dauria ground squirrels.Comp Biochem Physiol A Mol Integr Physiol 161, 296–300. https://doi.org/10.1016/j.cbpa.2011.11.009
72 Gellman, K.S., Bertram, J.E.A., Hermanson, J.W., 2002. Morphology, histochemistry, and function of epaxial cervical musculature in the horse (Equus caballus). J Morphol 251, 182–194. https://doi.org/10.1002/jmor.1082
73 Gibson, M.C., Schultz, E., 1982. The distribution of satellite cells and their relationship to specific fiber types in soleus and extensor digitorum longus muscles. Anat Rec 202, 329–337. https://doi.org/10.1002/ar.1092020305
74 Gillespie, M.J., Gordon, T., Murphy, P.R., 1987. Motor units and histochemistry in rat lateral gastrocnemius and soleus muscles: evidence for dissociation of physiological and histochemical properties after reinnervation. J Neurophysiol 57, 921–937. https://doi.org/10.1152/jn.1987.57.4.921
75 Goldstein, B., 1971. Heterogeneity of Muscle Fibers in Some Burrowing Mammals. J Mammal 52, 515–527. https://doi.org/10.2307/1378586
76 Gómez, M., Casado, A., de Diego, M., Pastor, J.F., Potau, J.M., 2022. Anatomical and molecular analyses of the deltoid muscle in chimpanzees (Pan troglodytes) and modern humans (Homo sapiens): Similarities and differences due to the uses of the upper extremity. Am J Primatol 84. https://doi.org/10.1002/ajp.23390
77 Gonyea, W.J., Ericson, G.C., 1977. Morphological and histochemical organization of the flexor carpi radialis muscle in the cat. Am J Anat 148, 329–344. https://doi.org/10.1002/aja.1001480304
78 Gorza, L., 1990. Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies. J Histochem Cytochem 38, 257–265. https://doi.org/10.1177/38.2.2137154
79 Goto, M., Itamoto, K., Tani, Y., Miyata, H., Kihara, I., Mori, F., Tajima, T., Wada, N., 2013a. Distribution of Muscle Fibers in Skeletal Muscles of the African Elephant (Loxodonta africana africana). Mammal Study 38, 135. https://doi.org/10.3106/041.038.0210
80 Goto, M., Kawai, M., Nakata, M., Itamoto, K., Miyata, H., Ikebe, Y., Tajima, T., Wada, N., 2013b. Distribution of muscle fibers in skeletal muscles of the cheetah (Acinonyx jubatus). Mamm Biol 78, 127–133. https://doi.org/10.1016/j.mambio.2012.07.001
81 Gotoh, T., 2003. Histochemical properties of skeletal muscles in Japanese cattle and their meat production ability, Anim Sci J.
82 Gray, S.D., Renkin, E.M., 1978. Microvascular supply in relation to fiber metabolic type in mixed skeletal muscles of rabbits. Microvasc Res 16, 406–425. https://doi.org/10.1016/0026-2862(78)90073-0
83 Graziotti, G.H., Chamizo, V.E., Ríos, C., Acevedo, L.M., Rodríguez-Menéndez, J.M., Victorica, C., Rivero, J.L.L., 2012. Adaptive functional specialisation of architectural design and fibre type characteristics in agonist shoulder flexor muscles of the llama, Lama glama. J Anat 221, 151–163. https://doi.org/10.1111/j.1469-7580.2012.01520.x
84 Graziotti, G.H., Palencia, P., Delhon, G., Rivero, J.L.L., 2004. Neuromuscular partitioning, architectural design, and myosin fiber types of the M. vastus lateralis of the llama (Lama glama). J Morphol 262, 667–681. https://doi.org/10.1002/jmor.10268
85 Graziotti, G.H., Ríos, C.M., Rivero, J.-L.L., 2001. Evidence for Three Fast Myosin Heavy Chain Isoforms in Type II Skeletal Muscle Fibers in the Adult Llama ( Lama glama ), J Histochem Cytochem.
86 Green, H.J., Klug, G.A., Reichmann, H., Seedorf, U., Wiehrer, W., Pette, D., 1984. Exercise-induced fibre type transitions with regard to myosin, parvalbumin, and sarcoplasmic reticulum in muscles of the rat. Pflug Arch Eur J Physiol 400, 432–8. https://doi.org/10.1007/BF00587545
87 Grotmol, S., Totland, G.K., Kryvi, H., Breistøl, A., Essén-Gustavsson, B., Lindholm, A., 2002. Spatial distribution of fiber types within skeletal muscle fascicles from standardbred horses. Anat Rec 268, 131–136. https://doi.org/10.1002/ar.10140
88 Hämäläinen, N., Pette, D., 1993. The histochemical profiles of fast fiber types IIB, IID, and IIA in skeletal muscles of mouse, rat, and rabbit. J Histochem Cytochem 41, 733–743. https://doi.org/10.1177/41.5.8468455
89 Hansen, S., Cutts, J.H., Krause, W.J., Cutts, J.H., 1987. Distribution of fibre types in thirty-seven muscles of Didelphis virginiana. Anat Anz 164, 153–8.
90 Hazimihalis, P.J., Gorvet, M.A., Butcher, M.T., 2013. Myosin Isoform Fiber Type and Fiber Size in the Tail of the Virginia Opossum (Didelphis virginiana). Anat Rec 296, 96–107. https://doi.org/10.1002/ar.22614
91 Hemingway, H.W., Burrows, A.M., Omstead, K.M., Zohdy, S., Pastor, J.F., Muchlinski, M.N., 2020. Vertical Clinging and Leaping Ahead: How Bamboo Has Shaped the Anatomy and Physiology of Hapalemur. Anat Rec 303, 295–307. https://doi.org/10.1002/ar.24183
92 Hena, S., Sonfada, M., Shehu, S., Jibir, M., Bello, A., Omirinde, J., Gosomji, I., 2018. Determination of the Proportions of Muscle Fibre Types from Selected Muscles of the Forelimb: A Comparative Study of Cattle (Bos taurus indicus) and One-humped Camel (Camelus dromedaries). J Vet Anat 11, 39–52. https://doi.org/10.21608/jva.2018.45055
93 Hermanson, J.W., Cobb, M.A., Schutt, W.A., Muradali, F., Ryan, J.M., 1993. Histochemical and myosin composition of vampire bat (Desmodus rotundus) pectoralis muscle targets a unique locomotory niche. J Morphol 217, 347–356. https://doi.org/10.1002/jmor.1052170309
94 Hermanson, J.W., Foehring, R.C., 1988. Histochemistry of flight muscles in the jamaican fruit bat, Artibeus jamaicensis: Implications for motor control. J Morphol 196, 353–362. https://doi.org/10.1002/jmor.1051960308
95 Hermanson, J.W., LaFramboise, W.A., Daood, M.J., 1991. Uniform myosin isoforms in the flight muscles of little brown bats,Myotis lucifugus. J Exp Zool 259, 174–180. https://doi.org/10.1002/jez.1402590205
96 Hermanson, J.W., Ryan, J.M., Cobb, M.A., Bentley, J., Schutts, Jr., W.A., 1998. Histochemical and electrophoretic analysis of the primary flight muscle of several phyllostomid bats. Can J Zool 76, 1983–1992. https://doi.org/10.1139/z98-158
97 Hershey, J.D., Robbins, C.T., Nelson, O.L., Lin, D.C., 2008. Minimal seasonal alterations in the skeletal muscle of captive brown bears. Physiol Biochem Zool 81, 138–147. https://doi.org/10.1086/524391
98 Hesse, B., Fischer, M.S., Schilling, N., 2010. Distribution pattern of muscle fiber types in the perivertebral musculature of two different sized species of mice. Anat Rec 293, 446–63. https://doi.org/10.1002/ar.21090
99 Hesse, B., Fröber, R., Fischer, M.S., Schilling, N., 2013. Functional differentiation of the human lumbar perivertebral musculature revisited by means of muscle fibre type composition. Ann Anat 195, 570–580. https://doi.org/10.1016/j.aanat.2013.07.003
100 Hitomi, Y., Kizaki, T., Watanabe, S., Matsumura, G., Fujioka, Y., Haga, S., Izawa, T., Taniguchi, N., Ohno, H., 2005. Seven skeletal muscles rich in slow muscle fibers may function to sustain neutral position in the rodent hindlimb. Comp Biochem Physiol B Biochem Mol Biol 140, 45–50. https://doi.org/10.1016/j.cbpc.2004.09.021
101 Ho, K.W., Heusner, W.W., van Huss, J., van Huss, W.D., 1983. Postnatal muscle fibre histochemistry in the rat. J Embryol Exp Morphol 76, 37–49.
102 Hochachka, P.W., Foreman III, R.A., 1993. Phocid and cetacean blueprints of muscle metabolism. Can J Zool 71, 2089–2098. https://doi.org/10.1139/z93-294
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