scholarly journals Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3

PLoS ONE ◽  
2016 ◽  
Vol 11 (11) ◽  
pp. e0165921 ◽  
Author(s):  
Congmin Li ◽  
Sunghyuk Lim ◽  
Karl H. Braunewell ◽  
James B. Ames
1980 ◽  
Vol 255 (2) ◽  
pp. 638-645 ◽  
Author(s):  
L.S. Hibbard ◽  
K.G. Mann

1996 ◽  
Vol 255 (1) ◽  
pp. 22-27 ◽  
Author(s):  
Vroni Knott ◽  
Kristina A. Downing ◽  
Caroline M. Cardy ◽  
Penny Handford

1994 ◽  
Vol 62 (12) ◽  
pp. 5220-5226 ◽  
Author(s):  
Y Duan ◽  
E Fisher ◽  
D Malamud ◽  
E Golub ◽  
D R Demuth

1994 ◽  
Vol 81 (SUPPLEMENT) ◽  
pp. A886
Author(s):  
T. J. J. Blanck ◽  
A. Levin

Author(s):  
J. Stenflo ◽  
M. Selander ◽  
E. Persson ◽  
J. Astermark ◽  
C. Valcarce ◽  
...  

1981 ◽  
Vol 22 (5-6) ◽  
pp. 653-657 ◽  
Author(s):  
Willem Nieuwenhuizen ◽  
Irina A.M. van Ruijven-Vermeer ◽  
Willem J. Nooijen ◽  
Anton Vermond ◽  
Frits Haverkate ◽  
...  

1980 ◽  
Vol 185 (1) ◽  
pp. 265-268 ◽  
Author(s):  
J Wikman-Coffelt

The non-specific Ca2+-binding sites of skeletal-muscle myosin are located on the light chains; with the dissociation of light chains there is a corresponding decrease in the number of Ca2+-binding sites on light-chain-deficient myosin. The released light chains have a decreased binding affinity. Myosin heavy chains indirectly influence the Ca2+-binding properties of light chains by increasing the affinity of light chains for bivalent cations; this influence varies with pH. Because of light-chain dissociation at low Ca2+ and/or Mg2+ concentrations, anomalies may exist when analyses of non-specific Ca2+-binding properties of myosin are assessed by dialysis equilibrium.


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