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1

Coluccio, Lynne M., ed. Myosins. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-38062-5.

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2

Coluccio, Lynne M. Myosins. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6519-4.

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3

Myosins. 2nd ed. Oxford: Oxford University Press, 1999.

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4

1933-, Sugi Haruo, and Pollack Gerald H, eds. Mechanism of myofilament sliding in muscle contraction. New York: Plenum Press, 1993.

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5

Sellers, James R. Motor proteins 2: myosin. London: Academic Press, 1995.

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6

A, Cross R., and Kendrick-Jones J, eds. Motor proteins: A volume based on the EMBO Workshop, Cambridge, September 1990. Cambridge [England]: Company of Biologists, 1991.

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7

Syrový, Ivo. Kontraktilní bílkoviny a funkční požadavky svalu. Praha: Academia, 1985.

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8

Griffiths, Hazel Sylvia. Studies on the properties and function of myosin light chain kinase. Birmingham: University of Birmingham, 1986.

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9

Thomas, D. D. Molecular Interactions of Actin: Actin-Myosin Interaction and Actin-Based Regulation. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002.

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10

Keane, Anita M. Peptide mimetics of an actin-binding site on the myosin head. Birmingham: University of Birmingham, 1991.

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11

Milankov, Kosta. Immunocytochemical localization of actin and myosin within interphase nuclei in situ. Ottawa: National Library of Canada, 1993.

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12

Epp, Trevor Allan. Characterization of the human cardiac gas-myosin heavy chain gene. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1993.

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13

Eastwood, Anthony Michael. The use of peptide mimetics in defining the actin-myosin interaction. Birmingham: University of Birmingham, 1994.

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14

Haruo, Sugi, Pollack Gerald H, and Mechanism of Myofilament Sliding in Muscle Contraction (1991 : Hakone, Japan), eds. Mechanism of myofilament sliding in muscle contraction. New York: Plenum Press, 1993.

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15

J, Baskin Ronald, and Yeh Yin 1938-, eds. Optical studies of muscle cross-bridges. Boca Raton, Fla: CRC Press, 1987.

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16

Timpson, David Julian. Fine tuning the myosin motor: The role of the essential light chain. Birmingham: University of Birmingham, 1996.

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17

Brown, Wendy Elizabeth. Changes in the myosin isoforms expressed during transformation of skeletal muscle phenotype. Birmingham: University of Birmingham, 1985.

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18

Dunn, Shannon Elizabeth. Regulation of myosin heavy chain isoform expression in adult rat skeletal muscle fibers. Sudbury, Ont: Laurentian University Press, 1996.

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19

Williams, Karen Jayne. The expression of myosin heavy chain isoforms in adult and developing skeletal muscle. Birmingham: University of Birmingham, 1990.

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20

Smith, Kevin John. The use of peptide mimetics to investigate the interface between actin and myosin. Birmingham: University of Birmingham, 1992.

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21

1536-1584, Yi I., and Ki Tʻae-wan, eds. Chŏngŏn myosŏn: Yulgok Yi I ŭi Chungguk sisŏn. Sŏul-si: Pogosa, 1999.

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22

Kazuhiro, Kohama, and Sasaki Yasuharu, eds. Molecular mechanisms of smooth muscle contraction. Austin, Tex: R.G. Landes Co., 1999.

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23

Kim, T'ae-hwan. Yulgok sidae ŭi mihak. Chŏnju-si: Sina Ch'ulp'ansa, 2003.

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24

J, Staiger C., ed. Actin: A dynamic framework for multiple plant cell functions. Dordrecht: Kluwer Academic Publishers, 2000.

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25

Huang, Weei-Yuarn. Nucleosomal structure and functions: Characterization of the hamster cardiac myosin heavy chain genes DNase I hypersensitive sites. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1997.

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26

1933-, Sugi Haruo, and Fujihara Kagaku Zaidan, eds. Molecular and cellular aspects of muscle contraction. New York: Kluwer Academic/Plenum Publishers, 2003.

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27

Viau, François. Effects of neural activity on oxidative and glycolytic enzyme activity and myosin heavy chain expression within diaphragm muscle fibers. Sudbury, Ont: Laurentian University, 1999.

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28

Myllynen, Jenni Eileen. The effect of nerve-mediated activity on the expression of Muscle Regulatory Factor and Myosin Heavy Chain Protein mRNA transcripts. Sudbury, Ont: Laurentian University, Behavioural Neuroscience Program, 1997.

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29

Alessi, Dario R. Synthesis of a conformationally restricted spin-labelled analogue of ATP for the study of the motion and structure of the myosin crossbridges. Birmingham: University of Birmingham, 1991.

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30

Stål, Per. Characterization of human oro-facial and masticatory muscles with respect to fibre types, myosins and capillaries: Morphological, enzyme-hisotchemical, immuno-histochemical and biochemical investigations. Umeå, Sweden: Departments of Anatomy and Clinical Oral Physiology, Umeå University, 1994.

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31

David, Radin, ed. The Zen of Myoshin-ji comes to the West: 25 years of Joshu Roshi in America, 1962-1987. [Kyoto?: Rinzai-ji Inc.], 1987.

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32

1922-, Ebashi Setsurō, and Ohtsuki Iwao, eds. Regulatory mechanisms of striated muscle contraction. Tokyo: Springer, 2007.

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33

Coluccio, Lynne M. Myosins. Springer, 2008.

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34

Sellers, James R. Myosins (Protein Profile). Oxford University Press, USA, 1999.

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35

Kennedy, Daniel L. Photoaffinity labeling of the ATP binding site of skeletal myosin. 1992.

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36

Broadbent, David. Myosin: Biosynthesis, Classes and Function. Nova Science Publishers, Incorporated, 2018.

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37

Coluccio, Lynne M. Myosins: A Superfamily of Molecular Motors. Springer, 2010.

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38

Myosins: A superfamily of molecular motors. Dordrecht: Springer, 2008.

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39

Coluccio, Lynne M. Myosins: A Superfamily of Molecular Motors. Springer, 2020.

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40

Coluccio, Lynne M. Myosins: A Superfamily of Molecular Motors. Springer London, Limited, 2007.

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41

Cole, Douglas Gene. Photoaffinity labeling of the ATP binding site of gizzard myosin. 1990.

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42

Huston, Edward Evan. The use of rigid bifunctional cross-linking agents as probes of the flexibility of the head region of myosin. 1985, 1985.

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43

Wang, Donald. Interaction of ATP analogs with myosin. 1994.

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44

Motor proteins: A volume based on the EMBO Workshop, Cambridge, September 1990 (Journal of cell science). Company of Biologists, 1991.

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45

Neuron, Joan M. A fluorescence study of myosin's active site with ribose modified nucleotide analogues trapped by SH₁-SH₂ crosslinking or by addition of vanadate. 1989.

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46

Blank, Sally. Electrophoretic myosin isoforms of skeletal muscles and single muscle fibers. 1987.

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47

Visessanguan, Wonnop. Endogenous proteinase and myosin gelation of arrowtooth flounder (Atheresthes stomias). 1999.

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48

Mahmood, Riaz. Photoaffinity labeling of myosin subfragment-one with 3'(2')-0-(4-benzoyl) benzoyl adenosine 5'-triphosphate. 1985.

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49

Dogra, Rajna. The stability of fish muscle myosins and their proteolytic subfragments. University of Nottingham, 1991.

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50

Turner, Neil, and Bertrand Knebelmann. MYH9 and renal disease. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0342_update_001.

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Abstract:
MYH9 encodes one of three heavy chain isoforms for the non-muscle myosin II (NM II) molecule. NM II is involved in cell structure and shape and motility. Myosin II is very widely expressed but MYH9 is highly expressed in podocytes. MYH9 diseases are characterized by various combinations of autosomal dominant progressive, proteinuric renal disease, giant platelets with low platelet counts, progressive sensorineural hearing impairment, granulocyte inclusions, and in some patients also cataracts. Although the eponyms Epstein and Fechtner have been given to MYH9 renal syndromes, there is a spectrum of manifestations of MYH9 diseases that do not correlate perfectly with genotype. They are best described as MYH9-associated renal disease. The occurrence of progressive deafness and renal failure led to this condition being considered an Alport syndrome variant in the past, but phenotype as well as molecular genetics clearly separate the disorders.
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