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  1. Book: Skeletal muscle repair and regeneration

    Schiaffino, Stefano

    (Advances in muscle research ; 3)

    2008  

    Author's details ed. by Stefano Schiaffino
    Series title Advances in muscle research ; 3
    Collection
    Language English
    Size XIII, 379 S. : Ill., graph. Darst., 235 mm x 155 mm
    Publisher Springer
    Publishing place Dordrecht
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT015511354
    ISBN 978-1-402-06767-9 ; 978-1-4020-6767-9 ; 1-4020-6767-4 ; 1-402-06767-4 ; 9781402067686 ; 1402067682
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2008 A 2430 order for loan Magazin

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  2. Book ; Online: Skeletal Muscle Repair and Regeneration

    Schiaffino, Stefano / Partridge, Terence

    2008  

    Author's details by Stefano Schiaffino, Terence Partridge
    Keywords Cell biology ; Developmental biology ; Medicine ; Neurology ; Sports medicine
    Language English
    Publisher Springer Science+Business Media B.V
    Publishing place Dordrecht
    Document type Book ; Online
    HBZ-ID TT050387034
    ISBN 978-1-402-06767-9 ; 978-1-402-06768-6 ; 1-402-06767-4 ; 1-402-06768-2
    DOI 10.1007/978-1-4020-6768-6
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  3. Article ; Online: Muscle fiber type diversity revealed by anti-myosin heavy chain antibodies.

    Schiaffino, Stefano

    The FEBS journal

    2018  Volume 285, Issue 20, Page(s) 3688–3694

    Abstract: Different forms of myosin heavy chains (MyHCs), coded by a large family of sarcomeric MYH genes, are expressed in striated muscles. The generation of specific anti-MyHC antibodies has provided a powerful tool to define the fiber types present in skeletal ...

    Abstract Different forms of myosin heavy chains (MyHCs), coded by a large family of sarcomeric MYH genes, are expressed in striated muscles. The generation of specific anti-MyHC antibodies has provided a powerful tool to define the fiber types present in skeletal muscles, their functional properties, their response to conditions that affect muscle plasticity and their changes in muscle disorders. Cardiomyocyte heterogeneity has been revealed by the serendipitous observation that different MyHCs are present in atrial and ventricular myocardium and in heart conduction tissue. Developmental MyHCs present in embryonic and fetal/neonatal skeletal muscle are re-expressed during muscle regeneration and can be used to identify regenerating fibers in muscle diseases. MyHC isoforms provide cell type-specific markers to identify the signaling pathways that control muscle cell identity and are an essential reference to interpret the results of single-cell transcriptomics and proteomics.
    MeSH term(s) Animals ; Antibodies, Monoclonal/immunology ; Gene Expression Regulation, Developmental ; Humans ; Muscle Fibers, Skeletal/classification ; Muscle Fibers, Skeletal/cytology ; Muscle Fibers, Skeletal/immunology ; Muscle Fibers, Skeletal/metabolism ; Muscle, Skeletal/cytology ; Muscle, Skeletal/immunology ; Muscle, Skeletal/metabolism ; Myosin Heavy Chains/analysis ; Myosin Heavy Chains/genetics ; Myosin Heavy Chains/immunology ; Protein Isoforms
    Chemical Substances Antibodies, Monoclonal ; Protein Isoforms ; Myosin Heavy Chains (EC 3.6.4.1)
    Language English
    Publishing date 2018-05-24
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.14502
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Knockout of human muscle genes revealed by large scale whole-exome studies.

    Schiaffino, Stefano

    Molecular genetics and metabolism

    2018  Volume 123, Issue 4, Page(s) 411–415

    Abstract: Large scale whole-exome sequence studies have revealed that a number of individuals from different populations have predicted loss-of-function of different genes due to nonsense, frameshift, or canonical splice-site mutations. Surprisingly, many of these ...

    Abstract Large scale whole-exome sequence studies have revealed that a number of individuals from different populations have predicted loss-of-function of different genes due to nonsense, frameshift, or canonical splice-site mutations. Surprisingly, many of these mutations do not apparently show the deleterious phenotypic consequences expected from gene knockout. These homozygous null mutations, when confirmed, can provide insight into human gene function and suggest novel approaches to correct gene dysfunction, as the lack of the expected disease phenotype may reflect the existence of modifier genes that reveal potential therapeutic targets. Human knockouts complement the information derived from mouse knockouts, which are not always good models of human disease. We have examined human knockout datasets searching for genes expressed exclusively or predominantly in striated muscle. A number of well-known muscle genes was found in one or more datasets, including genes coding for sarcomeric myosins, components of the sarcomeric cytoskeleton, sarcoplasmic reticulum and plasma membrane, and enzymes involved in muscle metabolism. The surprising absence of phenotype in some of these human knockouts is critically discussed, focusing on the comparison with the corresponding mouse knockouts.
    MeSH term(s) Gene Knockdown Techniques ; Genome, Human ; Humans ; Muscle Proteins/antagonists & inhibitors ; Muscle Proteins/genetics ; Muscles/metabolism ; Muscular Diseases/genetics ; Muscular Diseases/pathology ; Phenotype ; Whole Exome Sequencing/methods
    Chemical Substances Muscle Proteins
    Language English
    Publishing date 2018-02-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1418518-0
    ISSN 1096-7206 ; 1096-7192
    ISSN (online) 1096-7206
    ISSN 1096-7192
    DOI 10.1016/j.ymgme.2018.02.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 617: Show issues Location:
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  5. Article ; Online: Losing pieces without disintegrating: Contractile protein loss during muscle atrophy.

    Schiaffino, Stefano

    Proceedings of the National Academy of Sciences of the United States of America

    2017  Volume 114, Issue 8, Page(s) 1753–1755

    Language English
    Publishing date 2017-02-21
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1700190114
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1148: Show issues Location:
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  6. Article ; Online: MYH13, a superfast myosin expressed in extraocular, laryngeal and syringeal muscles.

    Schiaffino, Stefano / Hughes, Simon M / Murgia, Marta / Reggiani, Carlo

    The Journal of physiology

    2023  Volume 602, Issue 3, Page(s) 427–443

    Abstract: MYH13 is a unique type of sarcomeric myosin heavy chain (MYH) first detected in mammalian extraocular (EO) muscles and later also in vocal muscles, including laryngeal muscles of some mammals and syringeal muscles of songbirds. All these muscles are ... ...

    Abstract MYH13 is a unique type of sarcomeric myosin heavy chain (MYH) first detected in mammalian extraocular (EO) muscles and later also in vocal muscles, including laryngeal muscles of some mammals and syringeal muscles of songbirds. All these muscles are specialized in generating very fast contractions while producing relatively low force, a design appropriate for muscles acting against a much lower load than most skeletal muscles inserting into the skeleton. The definition of the physiological properties of muscle fibres containing MYH13 has been complicated by the mixed fibre type composition of EO muscles and the coexistence of different MYH types within the same fibre. A major advance in this area came from studies on isolated recombinant myosin motors and the demonstration that the affinity of actin-bound human MYH13 for ADP is much weaker than those of fast-type MYH1 (type 2X) and MYH2 (type 2A). This property is consistent with a very fast detachment of myosin from actin, a major determinant of shortening velocity. The MYH13 gene arose early during vertebrate evolution but was characterized only in mammals and birds and appears to have been lost in some teleost fish. The MYH13 gene is located at the 3' end of the mammalian fast/developmental gene cluster and in a similar position to the orthologous cluster in syntenic regions of the songbird genome. MYH13 gene regulation is controlled by a super-enhancer in the mammalian locus and deletion of the neighbouring fast MYH1 and MYH4 genes leads to abnormal MYH13 expression in mouse leg muscles.
    MeSH term(s) Animals ; Humans ; Mice ; Actins/metabolism ; Mammals/metabolism ; Myosin Heavy Chains/genetics ; Myosin Heavy Chains/metabolism ; Myosins/metabolism ; Oculomotor Muscles/metabolism
    Chemical Substances Actins ; Myosin Heavy Chains (EC 3.6.4.1) ; Myosins (EC 3.6.4.1) ; MYH13 protein, human
    Language English
    Publishing date 2023-12-31
    Publishing country England
    Document type Journal Article
    ZDB-ID 3115-x
    ISSN 1469-7793 ; 0022-3751
    ISSN (online) 1469-7793
    ISSN 0022-3751
    DOI 10.1113/JP285714
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Muscle hypertrophy and muscle strength: dependent or independent variables? A provocative review.

    Reggiani, Carlo / Schiaffino, Stefano

    European journal of translational myology

    2020  Volume 30, Issue 3, Page(s) 9311

    Abstract: The question whether the muscle hypertrophy induced by resistance training, hormone administration or genetic manipulation is accompanied by a proportional increase in muscle strength is still open. This review summarizes and analyses data obtained in ... ...

    Abstract The question whether the muscle hypertrophy induced by resistance training, hormone administration or genetic manipulation is accompanied by a proportional increase in muscle strength is still open. This review summarizes and analyses data obtained in human and rodent muscles in studies that have monitored in parallel changes in muscle size and changes in muscle force, measured in isometric contractions in vivo, in isolated muscles ex vivo (in rodents) and in single muscle fibers. Although a general positive relation exists among the two variables, a number of studies show a clear dissociation with increase of muscle size with no change or even decrease in strength and, vice versa, increase in strength without increase in size. The possible mechanisms of such dissociation, which involves neural motor control and/or cellular and molecular adaptations of muscle fibers, are briefly discussed.
    Language English
    Publishing date 2020-09-09
    Publishing country Italy
    Document type Journal Article
    ZDB-ID 2545577-1
    ISSN 2037-7460 ; 2037-7452
    ISSN (online) 2037-7460
    ISSN 2037-7452
    DOI 10.4081/ejtm.2020.9311
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Muscle hypertrophy and muscle strength

    Carlos Reggiani / Stefano Schiaffino

    European Journal of Translational Myology (2020)

    dependent or independent variables? A provocative review

    2020  

    Abstract: The question whether the muscle hypertrophy induced by resistance training, hormone administration or genetic manipulation is accompanied by a proportional increase in muscle strength is still open. This review summarizes and analyses data obtained in ... ...

    Abstract The question whether the muscle hypertrophy induced by resistance training, hormone administration or genetic manipulation is accompanied by a proportional increase in muscle strength is still open. This review summarizes and analyses data obtained in human and rodent muscles in studies that have monitored in parallel changes in muscle size and changes in muscle force, measured in isometric contractions in vivo, in isolated muscles ex vivo (in rodents) and in single muscle fibers. Although a general positive relation exists among the two variables, a number of studies show a clear dissociation with increase of muscle size with no change or even decrease in strength and, vice versa, increase in strength without increase in size. The possible mechanisms of such dissociation, which involves neural motor control and/or cellular and molecular adaptations of muscle fibers, are briefly discussed.
    Keywords skeletal muscle ; hypertrophy ; resistance training ; contractile force ; Medicine ; R ; Human anatomy ; QM1-695
    Subject code 796 ; 610
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher PAGEPress Publications
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Tubular aggregates in skeletal muscle: just a special type of protein aggregates?

    Schiaffino, Stefano

    Neuromuscular disorders : NMD

    2012  Volume 22, Issue 3, Page(s) 199–207

    Abstract: Tubular aggregates are inclusions, usually found in type II muscle fibers and in males, consisting of regular arrays of tubules derived from the sarcoplasmic reticulum. Tubular aggregates are associated with a wide variety of muscle disorders, including ... ...

    Abstract Tubular aggregates are inclusions, usually found in type II muscle fibers and in males, consisting of regular arrays of tubules derived from the sarcoplasmic reticulum. Tubular aggregates are associated with a wide variety of muscle disorders, including poorly defined "tubular aggregate myopathies" characterized by weakness and/or myalgia and/or cramps, and are also present in different mouse models, including normal aging muscles. The mechanism(s) responsible for inducing the formation of these structures have not been identified, because of the slow time course of their development in vivo, several months in mice. However, identical structures are formed in a few hours in rat muscles kept in vitro in hypoxic medium. Here I suggest that tubular aggregates result from reshaping of sarcoplasmic reticulum caused by misfolding and aggregation of membrane proteins and thus represent a special type of "protein aggregates" due to altered proteostasis.
    MeSH term(s) Animals ; Humans ; Male ; Mice ; Microscopy, Electron ; Muscle Proteins/genetics ; Muscle Proteins/metabolism ; Muscle, Skeletal/ultrastructure ; Muscular Diseases/metabolism ; Mutation/genetics ; Rats ; Sarcoplasmic Reticulum/metabolism
    Chemical Substances Muscle Proteins
    Language English
    Publishing date 2012-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1077681-3
    ISSN 1873-2364 ; 0960-8966
    ISSN (online) 1873-2364
    ISSN 0960-8966
    DOI 10.1016/j.nmd.2011.10.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Molecular Mechanisms of Skeletal Muscle Hypertrophy.

    Schiaffino, Stefano / Reggiani, Carlo / Akimoto, Takayuki / Blaauw, Bert

    Journal of neuromuscular diseases

    2020  Volume 8, Issue 2, Page(s) 169–183

    Abstract: Skeletal muscle hypertrophy can be induced by hormones and growth factors acting directly as positive regulators of muscle growth or indirectly by neutralizing negative regulators, and by mechanical signals mediating the effect of resistance exercise. ... ...

    Abstract Skeletal muscle hypertrophy can be induced by hormones and growth factors acting directly as positive regulators of muscle growth or indirectly by neutralizing negative regulators, and by mechanical signals mediating the effect of resistance exercise. Muscle growth during hypertrophy is controlled at the translational level, through the stimulation of protein synthesis, and at the transcriptional level, through the activation of ribosomal RNAs and muscle-specific genes. mTORC1 has a central role in the regulation of both protein synthesis and ribosomal biogenesis. Several transcription factors and co-activators, including MEF2, SRF, PGC-1α4, and YAP promote the growth of the myofibers. Satellite cell proliferation and fusion is involved in some but not all muscle hypertrophy models.
    MeSH term(s) Humans ; Hypertrophy ; Muscle, Skeletal/metabolism ; Protein Biosynthesis ; Signal Transduction
    Language English
    Publishing date 2020-11-20
    Publishing country Netherlands
    Document type Journal Article ; Review
    ISSN 2214-3602
    ISSN (online) 2214-3602
    DOI 10.3233/JND-200568
    Database MEDical Literature Analysis and Retrieval System OnLINE

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