Academic literature on the topic 'Skeletal muscle of cattle'

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Journal articles on the topic "Skeletal muscle of cattle"

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MARTINS, T. S., L. M. P. SANGLARD, W. SILVA, M. L. CHIZZOTTI, M. M. LADEIRA, N. V. L. SERÃO, P. V. R. PAULINO, and M. S. DUARTE. "Differences in skeletal muscle proteolysis in Nellore and Angus cattle might be driven by Calpastatin activity and not the abundance of Calpain/Calpastatin." Journal of Agricultural Science 155, no. 10 (November 9, 2017): 1669–76. http://dx.doi.org/10.1017/s0021859617000715.

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SUMMARYThe present study aimed to explore the molecular factors underlying differences in Calpain/Calpastatin proteolytic system in Nellore and Angus cattle. Longissimus muscle samples were collected in Nellore (n = 6; body weight (BW) = 373 ± 37·3 kg) and Angus (n = 6; BW = 383 ± 23·9 kg) cattle at slaughter for analysis of gene and protein expression, and Calpastatin enzyme activity. Additionally, the myofibrillar fragmentation index was used to quantify the extension of proteolysis in longissimus muscle samples. A greater myofibrillar fragmentation was observed in skeletal muscle of Angus compared with Nellore cattle. Conversely, no differences were found between breeds for mRNA expression of Calpain 1 (CAPN1) and Calpastatin (CAST). Similarly, no differences were observed for the abundance of Calpain and Calpastatin proteins between skeletal muscles of Nellore and Angus cattle. Despite the lack of differences in mRNA and protein abundance, a greater activity of Calpastatin was observed in skeletal muscle of Nellore compared with Angus cattle. These data indicate that the greater proteolysis in skeletal muscle of Angus compared with Nellore cattle is mainly driven by a greater Calpastatin activity rather than Calpain or Calpastatin mRNA and protein expression.
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Abreu, Camila C., Patricia C. Blanchard, John M. Adaska, Robert B. Moeller, Mark Anderson, Mauricio A. Navarro, Santiago S. Diab, and Francisco A. Uzal. "Pathology of blackleg in cattle in California, 1991–2015." Journal of Veterinary Diagnostic Investigation 30, no. 6 (October 25, 2018): 894–901. http://dx.doi.org/10.1177/1040638718808567.

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Blackleg is an infectious disease of cattle and rarely other ruminants, produced by Clostridium chauvoei and characterized by necrotizing myositis. In most cases of blackleg, the large muscles of the pectoral and pelvic girdles are affected, with other skeletal muscles and the heart involved less frequently. We studied 29 blackleg cases selected from the archives of the California Animal Health and Food Safety Laboratory, 1991–2015. Immunohistochemistry was also evaluated to detect C. chauvoei in formalin-fixed, paraffin-embedded (FFPE) tissues of cattle. Nineteen animals had gross and/or microscopic lesions in both skeletal muscle and heart, 9 had lesions in the skeletal musculature alone, and 1 in the heart alone. Gross lesions in the skeletal musculature involved the following muscle groups: hindquarters ( n = 8), forequarters ( n = 5), neck ( n = 5), lumbar area ( n = 3), brisket ( n = 2), diaphragm ( n = 2), abdominal wall ( n = 1), thoracic wall ( n = 1), and tongue ( n = 1). Of the 20 animals that had lesions in the heart, 11 had pericarditis and myocarditis; 7 had pericarditis, myocarditis, and endocarditis; and 1 each had pericarditis and myocarditis. Immunohistochemistry was 100% sensitive to detect C. chauvoei in FFPE skeletal muscle and/or heart of cattle with blackleg. Simultaneous lesions in skeletal musculature and heart were relatively common in blackleg cases in California; the most affected skeletal muscles were those of the hindlimbs.
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Martyn, Julie K., John J. Bass, and Jenny M. Oldham. "Skeletal muscle development in normal and double-muscled cattle." Anatomical Record 281A, no. 2 (2004): 1363–71. http://dx.doi.org/10.1002/ar.a.20140.

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Moreno-Sánchez, Natalia, Julia Rueda, María J. Carabaño, Antonio Reverter, Sean McWilliam, Carmen González, and Clara Díaz. "Skeletal muscle specific genes networks in cattle." Functional & Integrative Genomics 10, no. 4 (June 4, 2010): 609–18. http://dx.doi.org/10.1007/s10142-010-0175-2.

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Costagliola, A., S. Wojcik, T. B. Pagano, D. De Biase, V. Russo, V. Iovane, E. Grieco, S. Papparella, and O. Paciello. "Age-Related Changes in Skeletal Muscle of Cattle." Veterinary Pathology 53, no. 2 (February 11, 2016): 436–46. http://dx.doi.org/10.1177/0300985815624495.

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Antonelli, A. C., G. A. S. Torres, P. C. Soares, C. S. Mori, M. C. A. Sucupira, and E. L. Ortolani. "Ammonia poisoning causes muscular but not liver damage in cattle." Arquivo Brasileiro de Medicina Veterinária e Zootecnia 59, no. 1 (February 2007): 8–13. http://dx.doi.org/10.1590/s0102-09352007000100002.

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Twelve steers were intraruminally administered a high dose (0.5g/kg BW) of urea to study the damage effect of ammonia poisoning on liver and/or muscles. Blood samples were collected to determine ammonia and activities of gammaGT, AST and CK. Eleven steers were successfully poisoned and treated properly, but one succumbed. Poisoned cattle showed high concentration of ammonia, and higher activities of AST and CK. The higher the ammonia, the greater were the activities of AST (r=0.59) and CK (r=0.61). The correlation between AST and CK was high and significant (r=0.80), but not between AST and gammaGT (r=0.19). The activities of AST and CK were higher after the beginning of the convulsive episodes due to ammonia poisoning. Those results showed that occurred muscle damage instead of liver damage since CK is a typical enzyme from skeletal muscle; AST is found either in skeletal muscle and hepatocytes, while gammaGT is present in hepatic cells.
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Sun, Yujia, Yaoyao Ma, Xinyi Wu, Tianqi Zhao, Lu Lu, and Zhangping Yang. "Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation." Agriculture 12, no. 9 (September 8, 2022): 1420. http://dx.doi.org/10.3390/agriculture12091420.

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Agricultural meat composition and quality are not independent of the effects of skeletal muscle growth and development in animals. Cofilin is distributed extensively in muscle and non-muscle cells, and its function is tightly regulated in the cell. Cofilin has two variants in mammals, cofilin-1 (CFL1, non-muscle type) and cofilin-2 (CFL2, muscle type), and has a dual function on skeletal muscle fibers. Our study examined the expression pattern of CFL1 and CFL2 in different fetal bovine, calf, and adult cattle tissues. The content of the CFL2 gene increased significantly with the increase in cattle age in muscle tissues; CFL1 showed the opposite trend. In muscle tissues, DNA methylation levels of CFL1 and CFL2 were high in fetal bovine, and the mRNA level of CFL2 was significantly lower compared to CFL1. However, DNA methylation levels of CFL2 were lower than CFL1, and the mRNA level of CFL2 was remarkably higher compared to CFL1 in adult cattle. Overexpression of CFL1 or knockdown CFL2 reduced the expression levels of muscle differentiation markers, i.e., MYOD, MYOG, and MYH3. Overexpression of CFL2 or knockdown CFL1 stimulated the expression of these marker genes. Therefore, CFL2 may be superior to CFL1 as a candidate gene for subsequent research on cattle genetics and breeding.
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Zheng, Y. C., Y. Q. Lin, Y. Yue, Y. O. Xu, and S. Y. Jin. "Expression profiles of myostatin and calpastatin genes and analysis of shear force and intramuscular fat content of yak longissimus muscle." Czech Journal of Animal Science 56, No. 12 (December 22, 2011): 545–50. http://dx.doi.org/10.17221/4417-cjas.

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The main objective of this study was to reveal the expression profiles of two negative regulators, myostatin (MSTN) and calpastatin (CAST)genes, of skeletal muscle growth in highland yaks (Bos grunniens). mRNA levels of both genes were quantified in different yak tissues by semi-quantitative RT-PCR to reveal the tissue expression pattern, and real-time quantitative RT-PCR was employed to compare the mRNA levels of MSTN and CAST in longissimus muscles of yaks at different ages and adult Yellow cattle. Intramuscular fat (IMF) content, tenderness and pH of longissimus muscle of yaks at different ages and of adult Yellow cattle were also measured. The results showed that MSTN and CAST expressions have tissue specificity and both exhibited a high level in longissimus muscle and a low level in adipose tissue. Yak calves had lower mRNA levels of both MSTN and CAST in longissimus muscle compared with adult yaks. The analysis of meat quality traits of longissimus muscle showed that the shear forces of raw longissimus muscle of yak calves were significantly lower than those of adult yaks and Yellow cattle, no significant difference was found between adult yaks and Yellow cattle of similar age. IMF content in longissimus muscle was lower in yaks than in Yellow cattle. Although yaks were smaller in body size than Yellow cattle, adult yaks showed lower levels of MSTN and similar level of CAST mRNA in longissimus muscle compared to Yellow cattle. These data indicate that the expression of both MSTN and CAST in longissimus muscle differs between adult yaks and yak calves, and the yak longissimus muscle shows a lower IMF content compared to cattle.  
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Favorit, Victoria, Wendy R. Hood, Andreas N. Kavazis, Patricia Villamediana, Kang Nian Yap, Hailey A. Parry, and Amy L. Skibiel. "Mitochondrial Bioenergetics of Extramammary Tissues in Lactating Dairy Cattle." Animals 11, no. 9 (September 9, 2021): 2647. http://dx.doi.org/10.3390/ani11092647.

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Lactation is physiologically demanding, requiring increased nutrient and energy use. Mammary and extramammary tissues undergo metabolic changes for lactation. Although it has long been recognized that mitochondria play a critical role in lactation, the mitochondrial adaptations for milk synthesis in supporting tissues, such as liver and skeletal muscle are relatively understudied. In this study, we assessed the mitochondrial function in these tissues across lactation in dairy cattle. Tissue biopsies were taken at 8 ± 2 d (early, n = 11), 75 ± 4 d (peak, n = 11) and 199 ± 6 d (late, n = 11) in milk. Early lactation biopsies were harvested from one group of cows and the peak and late biopsies from a second cohort. Milk yield (MY) was recorded at each milking and milk samples were collected for composition analysis. Mitochondrial efficiency was quantified as the respiratory control ratio (RCR), comparing maximal to resting respiration rates. Liver complex II RCR was positively associated with MY. Liver ROS emission increased across lactation whereas liver antioxidant activity was similar across lactation. No change was detected in skeletal muscle RCR or ROS emission, but muscle GPx activity decreased across lactation and muscle SOD was negatively associated with MY. Muscle oxidative damage was elevated at early and late lactation. Across lactation, genes involved in mitochondrial biogenesis were upregulated in the liver. Our results indicate that during lactation, liver mitochondrial biogenesis and efficiency are increased, which is associated with greater milk yield. In contrast, the mitochondrial efficiency in skeletal muscle remains consistent across lactation, but undergoes oxidative damage, which is associated with reduced antioxidant activity.
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Sun, Yujia, Tianqi Zhao, Yaoyao Ma, Xinyi Wu, Yongjiang Mao, Zhangping Yang, and Hong Chen. "New Insight into Muscle-Type Cofilin (CFL2) as an Essential Mediator in Promoting Myogenic Differentiation in Cattle." Bioengineering 9, no. 12 (November 25, 2022): 729. http://dx.doi.org/10.3390/bioengineering9120729.

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Meat quality and meat composition are not separated from the influences of animal genetic improvement systems; the growth and development of skeletal muscle are the primary factors in agricultural meat production and meat quality. Though the muscle-type cofilin (CFL2) gene has a crucial influence on skeletal muscle fibers and other related functions, the epigenetic modification mechanism of the CFL2 gene regulating meat quality remains elusive. After exploring the spatiotemporal expression data of CFL2 gene in a group of samples from fetal bovine, calf, and adult cattle, we found that the level of CFL2 gene in muscle tissues increased obviously with cattle age, whereas DNA methylation levels of CFL2 gene in muscle tissues decreased significantly along with cattle age by BSP and COBRA, although DNA methylation levels and mRNA expression levels basically showed an opposite trend. In cell experiments, we found that bta-miR-183 could suppress primary bovine myoblast differentiation by negatively regulated CFL2. In addition, we packaged recombinant adenovirus vectors for CFL2 gene knockout and overexpression and found that the CFL2 gene could promote the differentiation of primary bovine myoblasts by regulating marker genes MYOD, MYOG and MYH3. Therefore, CFL2 is an essential mediator for promoting myogenic differentiation by regulating myogenic marker genes in cattle myoblasts.
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Dissertations / Theses on the topic "Skeletal muscle of cattle"

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Castro, Fernanda Campos de Paiva. "Skeletal muscle protein degradation in beef cattle /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2004. http://uclibs.org/PID/11984.

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Terry, Emily Nicole. "Regulation of selected selenoproteins in porcine and bovine skeletal muscle." Online access for everyone, 2008. http://www.dissertations.wsu.edu/Thesis/Spring2008/e_terry_041108.pdf.

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Ranasinghesagara, Janaka C. Yao Gang. "Optical reflectance in fibrous tissues and skeletal muscles." Diss., Columbia, Mo. : University of Missouri--Columbia, 2008. http://hdl.handle.net/10355/6629.

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Title from PDF of title page (University of Missouri--Columbia, viewed on March 8, 2010). The entire thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file; a non-technical public abstract appears in the public.pdf file. Dissertation advisor: Dr. Gang Yao. Vita. Includes bibliographical references.
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Zhang, Yafei. "Role of the Sh3 and Cysteine-Rich Domain 3 (STAC3) Gene in Proliferation and Differentiation of Bovine Satellite Cells." Thesis, Virginia Tech, 2013. http://hdl.handle.net/10919/76864.

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The STAC3 gene is a functionally undefined gene predicted to encode a protein containing two SH3 domains and one cysteine-rich domain. In this study, we determined the potential role of the STAC3 gene in proliferation and differentiation of bovine satellite cells. We isolated satellite cells from skeletal muscle of adult cattle and transfected them with STAC3 small interfering RNA (siRNA) or scrambled siRNA. Cell proliferation assays revealed that STAC3 knockdown had no effect on the proliferation rate of bovine satellite cells. We assessed the differentiation status of bovine satellite cells by quantifying the expression levels of myogenin and myosin heavy chain genes, and by quantifying fusion index. STAC3 knockdown stimulated mRNA and protein expression of myogenin, and myosin heavy chain 3 and 7, and increased fusion index of bovine satellite cells. These data together suggest that STAC3 inhibits differentiation of bovine satellite cells into myotubes. To determine the underlying mechanism, we identified and validated AP1?1 as a STAC3-interacting protein by yeast two-hybrid screening and co-immunoprecipitation. In C2C12 cells, STAC3 knockdown decreased the expression level of AP1?1 protein. In bovine satellite cells, STAC3 knockdown increased the membrane localization of glucose transporter 4 (GLUT4) and glucose uptake. These data together suggest the following mechanism by which STAC3 inhibits differentiation of bovine satellite cells: STAC3 increases AP1?1 stability in cells; a high level of AP1?1 keeps GLUT4 from translocating to the plasma membrane; reduced membrane localization of GLUT4 impedes glucose uptake; and restricted glucose uptake inhibits differentiation of satellite cells into myotubes.
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Baxa, Timothy John. "Effect of Zilpaterol hydrochloride and steroid implantation on yearling steer feedlot performance, carcass characteristics, and skeletal muscle gene expression." Thesis, Manhattan, Kan. : Kansas State University, 2008. http://hdl.handle.net/2097/936.

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Foxton, Ruth. "Dysferlin in skeletal muscle and skeletal muscle disease." Thesis, University of Newcastle Upon Tyne, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.268429.

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Peoples, Gregory Edward. "Skeletal muscle fatigue can omega-3 fatty acids optimise skeletal muscle function? /." Access electronically, 2004. http://www.library.uow.edu.au/adt-NWU/public/adt-NWU20041217.123607.

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Thesis (Ph.D.)--University of Wollongong, 2004.
Typescript. This thesis is subject to a 12 month embargo (06/09/05 - 14/09/05) and may only be viewed and copied with the permission of the author. For further information please contact the Archivist. Includes bibliographical references: leaf 195-216.
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Salman, Mahmoud M. "Preconditioning in skeletal muscle." Thesis, University College London (University of London), 2008. http://discovery.ucl.ac.uk/1446109/.

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Ischaemia reperfusion injury of skeletal muscle is a major cause of morbidity and mortality in various surgical specialities. Developing a protective method or pharmacological agent that will limit this damage will be of considerable benefit to both patients and doctors. I have used potassium channel openers and calcium as preconditioning agents. The results show that potassium channel openers are a viable option whereas the use of calcium can exacerbate muscle damage. I looked at various protocols of ischaemic and pharmacological preconditioning. The results from both ischaemic and pharmacological preconditioning have shown a comparable decrease with some pharmacological agents in the extent of skeletal muscle infarction both in the early and late period of reperfusion. This decrease in the extent of muscle infarction is associated with changes in the levels of nitric oxide in the circulation. There was preservation of skeletal muscle oxygenation in preconditioned muscle. I have shown that preconditioning of skeletal muscle is a viable option in trying to reduce the amount of damage caused by ischaemia reperfusion injury.
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Blackwell, Danielle. "The role of Talpid3 in skeletal muscle satellite cells and skeletal muscle regeneration." Thesis, University of East Anglia, 2017. https://ueaeprints.uea.ac.uk/66948/.

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The primary cilium has recently been recognised as an essential regulator of the Sonic hedgehog (Shh) signalling pathway. Mutations that disrupt cilia function in humans can cause conditions known as ciliopathies. A wide range of phenotypes is observed in chick and mouse ciliopathy models,including polydactyly, craniofacial defects and polycystic kidneys. The Shh pathway and therefore primary cilia are vital for many developmental processes, including embryonic muscle development, with recent evidence suggesting they may also play a role in adult muscle regeneration. Our studies focus on the Talpid3 gene, which encodes a centrosomal protein required for primary cilia formation and Shh signalling. The Talpid3 loss-of-function mutant has perturbed ciliogenesis and displays many of the phenotypes that are typically associated with developmental Shh mutants and with ciliopathies. Talpid3 mutants have defects in Shh signalling, and processing of Gli transcription factors is affected in structures such as the developing limb buds and the neural tube. However, the role of Talpid3 in muscle development and regeneration remains unknown. The role of Talpid3 in adult muscle regeneration was investigated using a tamoxifen inducible, satellite cell specific knock-out of Talpid3 in mice. This mouse model was generated by crossing Talpid3 floxed mice to a mouse carrying an inducible Pax7-CreERT2 allele. To determine whether loss of Talpid3 affects muscle regeneration a cardiotoxin injury model was used. This showed that loss of Talpid3 in satellite cells results in a regeneration defect as fibres were smaller after 5, 10, 15 and 25 days of regeneration compared to control mice. This defect may be due to a reduced ability of Talpid3 mutant satellite cells to differentiate. We also show that Talpid3 plays a role in satellite cell self-renewal as we observe a complete loss of regeneration in some areas of the muscle following repeat injuries. We provide the first evidence that Talpid3 is critical for the regeneration of skeletal muscle following injury.
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Zhang, Yan. "Cytokines and skeletal muscle wasting." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/MQ47124.pdf.

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Books on the topic "Skeletal muscle of cattle"

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Schmalbruch, Henning. Skeletal muscle. Berlin: Springer-Verlag, 1985.

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Schmalbruch, Henning. Skeletal Muscle. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-82551-4.

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Ryall, James G., ed. Skeletal Muscle Development. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7283-8.

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1957-, Prilutsky Boris I., ed. Biomechanics of skeletal muscle. Champaign, IL: Human Kinetics, 2012.

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International Congress on Myocardial and Cellular Bioenergetics and Compartmentation (2nd 1984 University of Southern California). Myocardial and skeletal muscle bioengertius. New York: Plenum, 1986.

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Anderson, Stephen Ian. Studies in skeletal muscle ischaemia. Birmingham: University of Birmingham, 1999.

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1955-, Tiidus Peter M., ed. Skeletal muscle damage and repair. Champaign, IL: Human Kinetics, 2008.

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1955-, Herzog W., ed. Theoretical models of skeletal muscle. Chichester: Wiley, 1998.

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Stefano, Schiaffino, and Partridge Terence, eds. Skeletal muscle repair and regeneration. Dordrecht: Springer, 2008.

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Atlas of skeletal muscle pathology. Lancaster: MTP Press, 1985.

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Book chapters on the topic "Skeletal muscle of cattle"

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Lancaster, P. A., M. A. Vaughn, J. D. Starkey, E. D. Sharman, C. R. Krehbiel, and G. W. Horn. "Growth rate in beef cattle affects adipose gene expression and skeletal muscle fiber type." In Energy and protein metabolism and nutrition in sustainable animal production, 389–90. Wageningen: Wageningen Academic Publishers, 2013. http://dx.doi.org/10.3920/978-90-8686-781-3_138.

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Fung, Yuan-Cheng. "Skeletal Muscle." In Biomechanics, 392–426. New York, NY: Springer New York, 1993. http://dx.doi.org/10.1007/978-1-4757-2257-4_9.

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Blottner, Dieter, and Michele Salanova. "Skeletal Muscle." In The NeuroMuscular System: From Earth to Space Life Science, 9–62. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-12298-4_2.

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Ding, Juan, and John J. Kopchick. "Skeletal Muscle." In Laron Syndrome - From Man to Mouse, 465–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-11183-9_53.

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Plonsey, Robert, and Roger C. Barr. "Skeletal Muscle." In Bioelectricity, 329–43. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4757-3152-1_11.

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Billings, Allison. "Skeletal Muscle." In Equine Clinical Pathology, 153–79. Chichester, UK: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118718704.ch9.

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Stiber, Jonathan A., and Paul B. Rosenberg. "Skeletal Muscle." In Store-operated Ca2+ entry (SOCE) pathways, 435–47. Vienna: Springer Vienna, 2011. http://dx.doi.org/10.1007/978-3-7091-0962-5_27.

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Ruegg, Urs T., George Shapovalov, Karin Jacobson, Julie Reutenauer-Patte, Hesham Ismail, Olivier M. Dorchies, and Pavel Avdonin. "Skeletal Muscle." In Store-operated Ca2+ entry (SOCE) pathways, 449–60. Vienna: Springer Vienna, 2011. http://dx.doi.org/10.1007/978-3-7091-0962-5_28.

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van der Ven, Peter F. M. "Skeletal Muscle." In Human Cell Culture, 65–101. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/0-306-46870-0_5.

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Plonsey, Robert, and Roger C. Barr. "Skeletal Muscle." In Bioelectricity, 259–70. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4757-9456-4_11.

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Conference papers on the topic "Skeletal muscle of cattle"

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NAGATOMI, RYOICHI. "SKELETAL MUSCLE AND HEALTH." In Proceedings of the Tohoku University Global Centre of Excellence Programme. IMPERIAL COLLEGE PRESS, 2012. http://dx.doi.org/10.1142/9781848169067_0003.

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Krivoi, Igor. "ENDOGENOUS OUABAIN AND SKELETAL MUSCLE." In XV International interdisciplinary congress "Neuroscience for Medicine and Psychology". LLC MAKS Press, 2019. http://dx.doi.org/10.29003/m446.sudak.ns2019-15/245-246.

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Burmeister and Lehman. "Force Relaxation In Human Skeletal Muscle." In Proceedings of the Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 1992. http://dx.doi.org/10.1109/iembs.1992.589829.

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Burmeister, E. E., and S. L. Lehman. "Force relaxation in human skeletal muscle." In 1992 14th Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 1992. http://dx.doi.org/10.1109/iembs.1992.5761946.

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Odegard, G. M., T. L. Haut Donahue, D. A. Morrow, and K. R. Kaufman. "Constitutive Modeling of Skeletal Muscle Tissue." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-175848.

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The main functions of the human musculoskeletal system are to sustain loads and provide mobility. Bones and joints themselves cannot produce movement; skeletal muscles provide the ability to move. Knowledge of muscle forces during given activities can provide insight into muscle mechanics, muscle physiology, musculoskeletal mechanics, neurophysiology, and motor control. However, clinical examinations or instrumented strength testing only provides information regarding muscle groups. Musculoskeletal models are typically needed to calculate individual muscle forces.
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Pohle, Regina, Ludwig von Rohden, and Dagmar Fisher. "Skeletal muscle sonography with texture analysis." In Medical Imaging 1997, edited by Kenneth M. Hanson. SPIE, 1997. http://dx.doi.org/10.1117/12.274164.

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Jaramillo, Paola, Adam Shoemaker, Alexander Leonessa, and Robert W. Grange. "Skeletal Muscle Contraction in Feedback Control." In ASME 2012 5th Annual Dynamic Systems and Control Conference joint with the JSME 2012 11th Motion and Vibration Conference. ASME, 2012. http://dx.doi.org/10.1115/dscc2012-movic2012-8592.

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Neal, Devin, Mahmut Selman Sakar, and H. Harry Asada. "Bioengineered Fascicle-Like Skeletal Muscle Tissue Constructs." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80228.

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Tissue engineered skeletal muscle constructs have and will continue to be valuable in treating, and testing various muscle injuries and diseases. However a significant drawback to numerous methods of producing 3D skeletal muscle constructs grown in vitro is that muscle cell density as a fraction of total volume or mass, is often significantly lower than muscle found in vivo. Therefore a method to increase muscle cell density within a construct is needed.
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Dudley, Gary A. "Skeletal Muscle Responses to Unweighting in Humans." In International Conference On Environmental Systems. 400 Commonwealth Drive, Warrendale, PA, United States: SAE International, 1991. http://dx.doi.org/10.4271/911462.

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Shuaib, Ali, Xin Li, and Gang Yao. "Polarization-Sensitive Transmittance Imaging in Skeletal Muscle." In Biomedical Optics. Washington, D.C.: OSA, 2010. http://dx.doi.org/10.1364/biomed.2010.btud63.

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Reports on the topic "Skeletal muscle of cattle"

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Walters, Thomas. Engineered Skeletal Muscle for Craniofacial Reconstruction. Fort Belvoir, VA: Defense Technical Information Center, November 2011. http://dx.doi.org/10.21236/ada601864.

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Buck, Edmond. Mechanism of Calcium Release from Skeletal Muscle Sarcoplasmic Reticulum. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.1306.

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Holdsworth, Clark, Steven Copp, Tadakatsu Inagaki, Daniel Hirai, Scott Ferguson, Gabrielle Sims, Michael White, David Poole, and Timothy Musch. Chronic (-)-epicatechin administration does not affect contracting skeletal muscle microvascular oxygenation. Peeref, May 2022. http://dx.doi.org/10.54985/peeref.2206p3750191.

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Koh, Timothy J. Enhancement of Skeletal Muscle Repair by the Urokinase-Type Plasminogen Activator System. Fort Belvoir, VA: Defense Technical Information Center, January 2006. http://dx.doi.org/10.21236/ada448526.

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Xiong, Hui. Modification of the CA²⁺ Release Channel from Sarcoplasmic Reticulum of Skeletal Muscle. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.1303.

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Wilmore, Douglas W. A Program for the Study of Skeletal Muscle Catabolism Following Physical Trauma. Fort Belvoir, VA: Defense Technical Information Center, November 1989. http://dx.doi.org/10.21236/ada216569.

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Wagner, Mark. The physiology and biochemistry of isolated skeletal muscle mitochondria : a comparative study. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5842.

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Stuart, Janice. Chemical Modification of Skeletal Muscle Sarcoplasmic Reticulum Vesicles: A Study of Calcium Permeability. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.1388.

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Goerke, Ute. Proteolytic modification of the Ca²-release mechanism of sarcoplasmic reticulum in skeletal muscle. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.6101.

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Dornan, Thomas. Antioxidant Anthocyanidins and Calcium Transport Modulation of the Ryanodine Receptor of Skeletal Muscle (RyR1). Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.319.

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