372
10 Proteins of Muscle and the Cytoskeleton
168. Lindenthal S. and Schubert D.: Monomeric erythrocyte band-3 protein transports anions. Proc. Nat.
Acad. Sci. USA 88: 6540-44 (1991)
169. Little M. and Seehaus T.: Comparative analysis of
tubulin sequences. Compo Biochem. PhysioI. Pt. B
90: 655-670 (1988)
170. Lucin S. V. et al.: Frog lens f3Al-crystallin: the nucleotide sequence of the cloned cDNA and computer
graphics modelling of the three-dimensional structure. Biochim. biophys. Acta 916: 163-171 (1987)
171. Lynch T. J. et aI.: Purification and characterization of
a third isoform of myosin I from Acanthamoeba castellanii. J. BioI. Chern. 264: 19333-39 (1989)
172. Maingon R. et al.: The tubulin genes of Trypanosoma
cruzi. Eur. J. Biochem. 171: 285-291 (1988)
173. Maita G., Maita T. and Umegane T.: The primary
structure of L-l light chain of chicken fast skeletal
muscle myosin and its genetic implication. FEBS Letters 126: 111-113 (1981)
174. Maita T., Chen J. I. and Matsuda G.: Amino-acid
sequence of the 20,OOO-molecular-weight light chain
of chicken gizzard-muscle myosin. Eur. J. Biochem.
117: 417-424 (1981)
175. Maita T. et aI.: The primary structure of the myosin
head. Proc. Nat. Acad. Sci. USA 84: 416-420 (1987)
176. Manseau L. J., Ganetzky B. and Craig E. A.: Molecular and genetic characterization of the Drosophila
melanogaster 87E actin gene region. Genetics 119:
407-420 (1988)
177. Martinez I. et aI.: Comparsison of myosin isoenzymes
present in skeletal and cardiac muscles of the Arctic
charr Salvelinus alpinus (L.). Sequential expression
of different myosin heavy chains during development
of the fast white skeletal muscle. Eur. J. Biochem.
195: 743-753 (1991)
178. Matsuda G. et al.: Amino acid sequences of the cardiac
L-2A, L-2B and gizzard 17,OOO-Mr light chains of chicken
muscle myosin. FEBS Letters 135: 232-236 (1981)
179. McIntosh J. R. and Porter M. E.: Enzymes for
microtubule-dependent motility. J. BioI. Chern. 264:
6001-04 (1989)
180. McKeon F. D., Kirschner M. W. and Caput D.:
Homologies in both primary and secondary structure
between nuclear envelope and intermediate filament
proteins. Nature 319: 463-468 (1986)
181. McNally E. M. et al.: Full-length rat alpha and beta
cardiac myosin heavy chain sequences. Comparisons
suggest a molecular basis for functional differences. J.
mol. BioI. 210: 665-671 (1989)
182. Michel F. and Rudloff V.: Isolation and characterization of the rainbow trout erythrocyte band-3 protein.
Eur. J. Biochem. 181: 181-187 (1989)
183. Millake D. B. et aI.: The cDNAsequence of a human
placental a-actinin. Nucleic Acids Res. 17: 6725 (1989)
184. Milner R. E. et aI.: Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth
muscle sarcoplasmic reticulum and liver endoplasmic
reticulum. J. BioI. Chern. 266: 7155-65 (1991)
185. Mimura T., Yamanobe T. and Sugi H.: Isolation and
characterization of calmodulin from a molluscan
smooth muscle. Compo Biochem. PhysioI. Pt. B 81:
559-563 (1985)
186. Miwa T. and Kamada S.: The nucleotide sequence of
a human smooth muscle (enteric type) gamma-actin
cDNA. Nucleic Acids Res. 18: 4263 (1990)
187. Miyazaki J. I., Sekiguchi K. and Hirabayashi T.: Tissue specificity of tropomyosin from a horseshoe crab,
Tachypleus tridentatus. Compo Biochem. PhysioI. Pt.
B 85: 679-685 (1986)
188. Mohun T. et al.: A third striated muscle actin gene is
expressed during early development in the amphibian
Xenopus laevis. J. mol. BioI. 202: 67-76 (1988)
189. Molina M. I. et al.: The sequence of an embryonic
myosin heavy chain gene and isolation of its corresponding cDNA. J. bioI. Chern. 262: 6478-88 (1987)
190. MoncriefN. D., Kretsinger R. H. and Goodman M.:
Evolution of EF-hand calcium-modulated proteins. I.
Relationships based on amino acid sequences. J. mol.
EvoI. 30: 522-562 (1990)
191. Moon R. T. and McMahon A. P.: Generation of
diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs
emcompassing the coding region of human nonerythroid a-spectrin. J. BioI. Chern. 265: 4427-33 (1990)
192. Moormann R. J. M. et al.: Strict co-linearity of genetic and protein folding domains in an intragenically
duplicated rat lens y-crystallin gene. J. mol. BioI. 171:
353-368 (1983)
193. Morishima I. and Bodnaryk R. P.: Amino acid composition of insect calmodulins lacking trimethyllysine.
Compo Biochem. PhysioI. Pt. B 80: 419-423 (1985)
194. Moriyama K. et al.: Destrin, a mammalian actindepolymerizing protein, is closely related to cofilin.
Cloning and expression of porcine brain destrin
cDNA. J. BioI. Chern. 265: 5768-73 (1990)
195. Morris G. L. et al.: Phospholamban regulation of cardiac sarcoplasmic reticulum (Ca-Mg)-ATPase. J.
BioI. Chern. 266: 11270-75 (1991)
196. Mounier N., Gaillard J. and Prudhomme J. C.: Nucleotide sequence of the coding region of two actin
genes in Bombyx mori. Nucleic Acids Res. 15: 2781
(1987)
197. Mulders J. W. M. et al.: lambda-Crystallin, a major
rabbit lens protein, is related to hydroxyacylcoenzyme A dehydrogenase. J. BioI. Chern. 263:
15462-66 (1988)
198. Murayama J. I., Utsumi H. and Hamada A.: Amino
acid sequence of monkey erythrocyte glycophorin
MK. Its amino acid sequence has a striking homology
with that of human glycophorin A. Biochim. biophys.
Acta 999: 273-280 (1989)
199. Murphy D. B. et al.: The sequence and expression of
the divergent f3-tubulin in chicken erythrocytes. J.
bioI. Chern. 262: 14305-12 (1987)
200. Myers M. W. et al.: The human mid-size neurofilament subunit: a repeated protein sequence and the
relationship of its gene to the intermediate filament
gene family. Embo J. 6: 1617-26 (1987)
201. Mykles D. L.: Heterogeneity of myofibrillar proteins in
lobster fast and slow muscles - Variants of troponin,
paramyosin, and myosin light chains comprise 4 distinct
protein assemblages. J. expo ZooI. 234: 23-32 (1985)
202. Nakajima-Iijima S. et aI.: Molecular structure of the
human cytoplasmic f3-actin gene: interspecies homology of sequence in the introns. Proc. Nat. Acad. Sci.
USA 82: 6133-37 (1985)
203. Nikovits jr. w., Kuncio G. and Ordahl C. P.: The
chicken fast skeletal muscle troponin I gene: exon
organization and sequence. Nucleic Acids Res. 14:
3377-90 (1986)
204. Nojima H.: Structural organization of multiple rat
calmodulin genes. J. mol. BioI. 208: 269-282 (1989)
205. Obar R. A. et al.: Molecular cloning of the
microtubule-associated mechanochemical enzyme
10 Proteins of Muscle and the Cytoskeleton
168. Lindenthal S. and Schubert D.: Monomeric erythrocyte band-3 protein transports anions. Proc. Nat.
Acad. Sci. USA 88: 6540-44 (1991)
169. Little M. and Seehaus T.: Comparative analysis of
tubulin sequences. Compo Biochem. PhysioI. Pt. B
90: 655-670 (1988)
170. Lucin S. V. et al.: Frog lens f3Al-crystallin: the nucleotide sequence of the cloned cDNA and computer
graphics modelling of the three-dimensional structure. Biochim. biophys. Acta 916: 163-171 (1987)
171. Lynch T. J. et aI.: Purification and characterization of
a third isoform of myosin I from Acanthamoeba castellanii. J. BioI. Chern. 264: 19333-39 (1989)
172. Maingon R. et al.: The tubulin genes of Trypanosoma
cruzi. Eur. J. Biochem. 171: 285-291 (1988)
173. Maita G., Maita T. and Umegane T.: The primary
structure of L-l light chain of chicken fast skeletal
muscle myosin and its genetic implication. FEBS Letters 126: 111-113 (1981)
174. Maita T., Chen J. I. and Matsuda G.: Amino-acid
sequence of the 20,OOO-molecular-weight light chain
of chicken gizzard-muscle myosin. Eur. J. Biochem.
117: 417-424 (1981)
175. Maita T. et aI.: The primary structure of the myosin
head. Proc. Nat. Acad. Sci. USA 84: 416-420 (1987)
176. Manseau L. J., Ganetzky B. and Craig E. A.: Molecular and genetic characterization of the Drosophila
melanogaster 87E actin gene region. Genetics 119:
407-420 (1988)
177. Martinez I. et aI.: Comparsison of myosin isoenzymes
present in skeletal and cardiac muscles of the Arctic
charr Salvelinus alpinus (L.). Sequential expression
of different myosin heavy chains during development
of the fast white skeletal muscle. Eur. J. Biochem.
195: 743-753 (1991)
178. Matsuda G. et al.: Amino acid sequences of the cardiac
L-2A, L-2B and gizzard 17,OOO-Mr light chains of chicken
muscle myosin. FEBS Letters 135: 232-236 (1981)
179. McIntosh J. R. and Porter M. E.: Enzymes for
microtubule-dependent motility. J. BioI. Chern. 264:
6001-04 (1989)
180. McKeon F. D., Kirschner M. W. and Caput D.:
Homologies in both primary and secondary structure
between nuclear envelope and intermediate filament
proteins. Nature 319: 463-468 (1986)
181. McNally E. M. et al.: Full-length rat alpha and beta
cardiac myosin heavy chain sequences. Comparisons
suggest a molecular basis for functional differences. J.
mol. BioI. 210: 665-671 (1989)
182. Michel F. and Rudloff V.: Isolation and characterization of the rainbow trout erythrocyte band-3 protein.
Eur. J. Biochem. 181: 181-187 (1989)
183. Millake D. B. et aI.: The cDNAsequence of a human
placental a-actinin. Nucleic Acids Res. 17: 6725 (1989)
184. Milner R. E. et aI.: Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth
muscle sarcoplasmic reticulum and liver endoplasmic
reticulum. J. BioI. Chern. 266: 7155-65 (1991)
185. Mimura T., Yamanobe T. and Sugi H.: Isolation and
characterization of calmodulin from a molluscan
smooth muscle. Compo Biochem. PhysioI. Pt. B 81:
559-563 (1985)
186. Miwa T. and Kamada S.: The nucleotide sequence of
a human smooth muscle (enteric type) gamma-actin
cDNA. Nucleic Acids Res. 18: 4263 (1990)
187. Miyazaki J. I., Sekiguchi K. and Hirabayashi T.: Tissue specificity of tropomyosin from a horseshoe crab,
Tachypleus tridentatus. Compo Biochem. PhysioI. Pt.
B 85: 679-685 (1986)
188. Mohun T. et al.: A third striated muscle actin gene is
expressed during early development in the amphibian
Xenopus laevis. J. mol. BioI. 202: 67-76 (1988)
189. Molina M. I. et al.: The sequence of an embryonic
myosin heavy chain gene and isolation of its corresponding cDNA. J. bioI. Chern. 262: 6478-88 (1987)
190. MoncriefN. D., Kretsinger R. H. and Goodman M.:
Evolution of EF-hand calcium-modulated proteins. I.
Relationships based on amino acid sequences. J. mol.
EvoI. 30: 522-562 (1990)
191. Moon R. T. and McMahon A. P.: Generation of
diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs
emcompassing the coding region of human nonerythroid a-spectrin. J. BioI. Chern. 265: 4427-33 (1990)
192. Moormann R. J. M. et al.: Strict co-linearity of genetic and protein folding domains in an intragenically
duplicated rat lens y-crystallin gene. J. mol. BioI. 171:
353-368 (1983)
193. Morishima I. and Bodnaryk R. P.: Amino acid composition of insect calmodulins lacking trimethyllysine.
Compo Biochem. PhysioI. Pt. B 80: 419-423 (1985)
194. Moriyama K. et al.: Destrin, a mammalian actindepolymerizing protein, is closely related to cofilin.
Cloning and expression of porcine brain destrin
cDNA. J. BioI. Chern. 265: 5768-73 (1990)
195. Morris G. L. et al.: Phospholamban regulation of cardiac sarcoplasmic reticulum (Ca-Mg)-ATPase. J.
BioI. Chern. 266: 11270-75 (1991)
196. Mounier N., Gaillard J. and Prudhomme J. C.: Nucleotide sequence of the coding region of two actin
genes in Bombyx mori. Nucleic Acids Res. 15: 2781
(1987)
197. Mulders J. W. M. et al.: lambda-Crystallin, a major
rabbit lens protein, is related to hydroxyacylcoenzyme A dehydrogenase. J. BioI. Chern. 263:
15462-66 (1988)
198. Murayama J. I., Utsumi H. and Hamada A.: Amino
acid sequence of monkey erythrocyte glycophorin
MK. Its amino acid sequence has a striking homology
with that of human glycophorin A. Biochim. biophys.
Acta 999: 273-280 (1989)
199. Murphy D. B. et al.: The sequence and expression of
the divergent f3-tubulin in chicken erythrocytes. J.
bioI. Chern. 262: 14305-12 (1987)
200. Myers M. W. et al.: The human mid-size neurofilament subunit: a repeated protein sequence and the
relationship of its gene to the intermediate filament
gene family. Embo J. 6: 1617-26 (1987)
201. Mykles D. L.: Heterogeneity of myofibrillar proteins in
lobster fast and slow muscles - Variants of troponin,
paramyosin, and myosin light chains comprise 4 distinct
protein assemblages. J. expo ZooI. 234: 23-32 (1985)
202. Nakajima-Iijima S. et aI.: Molecular structure of the
human cytoplasmic f3-actin gene: interspecies homology of sequence in the introns. Proc. Nat. Acad. Sci.
USA 82: 6133-37 (1985)
203. Nikovits jr. w., Kuncio G. and Ordahl C. P.: The
chicken fast skeletal muscle troponin I gene: exon
organization and sequence. Nucleic Acids Res. 14:
3377-90 (1986)
204. Nojima H.: Structural organization of multiple rat
calmodulin genes. J. mol. BioI. 208: 269-282 (1989)
205. Obar R. A. et al.: Molecular cloning of the
microtubule-associated mechanochemical enzyme