for structurally distinct proteins. Proc. Nat. Acad.
Sci. USA 83: 8477-81 (1986)
284. Tomarev S. I. and Zinovieva D.: Squid major lens
polypeptides are homologous to glutathione Stransferase subunits. Nature 336: 86-88 (1988)
285. Toyofuku T. and Zak R.: Characterization of cDNA
and genomic sequences encoding a chicken phospholamban. J. BioI. Chern. 266: 5375-83 (1991)
286. Toyoshima Y. Y., Kron S. J. and Spudich J. A.: The
myosin step size. Measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. Proc.
Nat. Acad. Sci. USA 87: 7130-34 (1990)
287. Treveso S. et al.: Frog brain expresses a 60 kDa
calcium-binding protein similar to mammalian calreticulin. Biochem. biophys. Res. Commun. 175:
444-450 (1991)
288. Vandekerckhove J. and Weber K.: Chordate muscle
actins differ distinctly from invertebrate muscle
actins. The evolution of the different vertebrate
muscle actins. J. mol. BioI. 179: 391-413 (1984)
289. Vandekerckhove J., Lal A. A. and Korn E. D.:
Amino acid sequence of Acanthamoeba actin. J. mol.
BioI. 172: 141-147 (1984)
290. Vandekerckhove J., Bugaisky G. and Buckingham
M.: Simultaneous expression of skeletal muscle and
heart actin proteins in various striated muscle tissues
and cells. A quantitative determination of the two
actin isoforms. J. bioI. Chern. 261: 1938-43 (1986)
291. Vignal A. et al.: A novel gene member of the human
glycophorin A and B gene family: Molecular cloning
and expression. Eur. J. Biochem. 191: 619-625 (1990)
292. Vilasante A. et al.: Six mouse a-tubulin mRNAs
encode five distinct isotypes: Testis-specific expression
of two sister genes. Mol cell. BioI. 6: 2409-19 (1986)
293. Volpe P. et al.: "Calciosome", a cytoplasmic organelle: the inositol 1,4,5-triphosphate-sensitive
Calcium-store of nonmuscle cells? Proc. Nat. Acad.
Sci. USA 85: 1091-95 (1988)
294. Volpe P. and Simon B. J.: The bulk of calcium
released to the myoplasm is free in the sarcoplasmic
reticulum and does not unbind from calsequestrin.
FEBS Letters 278: 274-278 (1991)
295. Voorter C. E. M. et al.: Age-dependent deamidation
of chicken aA-crystallin. FEBS Letters 221: 249-252
(1987)
296. Wang S. M., Sun M. C. and Jeng C. J.: Location of
the C-terminus of titin at the Z-line region in the sarcomere. Biochem. biophys. Res. Commun. 176:
189-193 (1991)
297. Ward S. et al.: Genomic organizations of major sperm
protein genes and pseudogenes in the nematode Caenorhabditis elegans. J. mol. BioI. 199: 1-13 (1988)
298. Wasenius V. M. et al.: a-Actinin and spectrin have
common structural domains. FEBS Letters 221:
73-76 (1987)
299. Watabe S. and Hartshorne D. J.: Paramyosin and the
catch mechanism. Compo Biochem. Physiol. Pt. B 96:
639-646 (1990)
300. Weber K., Plessmann U. and Ulrich w.: Cytoplasmic
intermediate filament proteins of invertebrates are
closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization
of two muscle proteins of a nematode. Embo J. 8:
3221-27 (1989)
301. Weeds A. G. et al.: Preparation and characteriziation
of pig plasma and platelet gelsolins. Eur. J. Biochem.
161: 69-76 (1986)
References
375
302. Weller P. A. et al.: Complete sequence of human vinculin and assignment of the gene to chromosome 10.
Proc. Nat. Acad. Sci. USA 87: 5667-71 (1990)
303. Wesseling J. G. et al.: Nucleotide sequence and
expression of a ~-tubulin-encoding gene from Plasmodium falciparum, a malarial parasite of man. Gene
83: 301-309 (1989)
304. Whitbread L. A., Gregg K. and Rogers G. E.: The
structure and expression of a gene encoding chick
claw keratin. Gene 101: 223-229 (1991)
305. Wiche G.: High-Mt microtubule-associated proteins:
properties and functions. Biochem. J. 259: 1-12 (1989)
306. Wilson P. W. et al.: Structure of chick chromosomal
genes for calbindin and calretinin. J. mol. BioI. 200:
615-625 (1988)
307. Winder S. J. and Walsh M. P.: Smooth muscle calponino Inhibition of actomyosin MgATPase and regulation by phosphorylation. J. BioI. Chern. 265:
10148-55 (1990)
308. Winkelmann J. C. et al.: Full-length sequence of the
cDNA for human erythroid ~-spectrin. J. BioI.
Chern. 265: 11827-32 (1990)
309. Winrow M. A. and Sodja A.: Initial characterization
of several actin genes in the parasitic nematode,
Ascaris suum. Biochem. biophys. Res. Commun.
178: 578-585 (1991)
310. Wistow G. J. and Piatigorsky J.: Gene conversion
and splice-site slippage in the argininosuccinate lyases
delta-crystallins of the duck lens: Members of an
enzyme superfamily. Gene 96: 263-270 (1990)
311. Wistow G., Anderson A. and Piatigorsky J.: Evidence for neutral and selective processes in the recruitment of enzyme-crystallins in avian lenses. Proc. Nat.
Acad. Sci. USA 87: 6277-80 (1990)
312. Wistow G. and Kim H.: Lens protein expression in
mammals. Taxon-specificity and the recruitment of
crystallins. J. mol. Evol. 32: 262-269 (1991)
313. Wohlfarth-Bottermann K. E. (ed.): Nature and function of cytoskeletal proteins in motility and transport.
G. Fischer, Stuttgart 1987
314. Xiang M. et al.: Tandem duplication and divergence
of a sea urchin protein belonging to the troponin C
superfamily. J. BioI. Chern. 263: 17173-80 (1988)
315. Yaffe D. et al.: Highly conserved sequences in the 3'
untranslated region of mRNAs coding for homologous proteins in distantly related species. Nucleic
Acids Res. 13: 3723-37 (1985)
316. Yamanaka M. K. et al.: Structure and expression of
the Drosophila calmodulin gene. Nucleic Acids Res.
15: 3335-48 (1987)
317. Yazaki P. J. et al.: Calsequestrin, an intracellular
calcium-binding protein of skeletal muscle sarcoplasmic reticulum, is homologous to aspartactin, a
putative laminin-binding protein of the extracellular
matrix. Biochem. biophys. Res. Commun. 166:
898-903 (1990)
318. Yazawa M. et al.: The amino acid sequence of the Tetrahymena calmodulin which specifically interacts with
guanylate cyclase. Biochem. biophys. Res. Commun.
99: 1051-57 (1981)
319. Zarain-Herzberg A., Fliegel L. and MacLennan D.
H.: Structure of the rabbit fast-twitch skeletal muscle
calsequestrin gene. J. BioI. Chern. 263: 4807-12
(1988)
320. Zehner Z. E. et al.: The chicken vimentin gene. Nucleotide sequence, regulatory elements, and comparison of
the hamster gene. J. bioI. Chern. 262: 8112-20 (1987)
Sci. USA 83: 8477-81 (1986)
284. Tomarev S. I. and Zinovieva D.: Squid major lens
polypeptides are homologous to glutathione Stransferase subunits. Nature 336: 86-88 (1988)
285. Toyofuku T. and Zak R.: Characterization of cDNA
and genomic sequences encoding a chicken phospholamban. J. BioI. Chern. 266: 5375-83 (1991)
286. Toyoshima Y. Y., Kron S. J. and Spudich J. A.: The
myosin step size. Measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. Proc.
Nat. Acad. Sci. USA 87: 7130-34 (1990)
287. Treveso S. et al.: Frog brain expresses a 60 kDa
calcium-binding protein similar to mammalian calreticulin. Biochem. biophys. Res. Commun. 175:
444-450 (1991)
288. Vandekerckhove J. and Weber K.: Chordate muscle
actins differ distinctly from invertebrate muscle
actins. The evolution of the different vertebrate
muscle actins. J. mol. BioI. 179: 391-413 (1984)
289. Vandekerckhove J., Lal A. A. and Korn E. D.:
Amino acid sequence of Acanthamoeba actin. J. mol.
BioI. 172: 141-147 (1984)
290. Vandekerckhove J., Bugaisky G. and Buckingham
M.: Simultaneous expression of skeletal muscle and
heart actin proteins in various striated muscle tissues
and cells. A quantitative determination of the two
actin isoforms. J. bioI. Chern. 261: 1938-43 (1986)
291. Vignal A. et al.: A novel gene member of the human
glycophorin A and B gene family: Molecular cloning
and expression. Eur. J. Biochem. 191: 619-625 (1990)
292. Vilasante A. et al.: Six mouse a-tubulin mRNAs
encode five distinct isotypes: Testis-specific expression
of two sister genes. Mol cell. BioI. 6: 2409-19 (1986)
293. Volpe P. et al.: "Calciosome", a cytoplasmic organelle: the inositol 1,4,5-triphosphate-sensitive
Calcium-store of nonmuscle cells? Proc. Nat. Acad.
Sci. USA 85: 1091-95 (1988)
294. Volpe P. and Simon B. J.: The bulk of calcium
released to the myoplasm is free in the sarcoplasmic
reticulum and does not unbind from calsequestrin.
FEBS Letters 278: 274-278 (1991)
295. Voorter C. E. M. et al.: Age-dependent deamidation
of chicken aA-crystallin. FEBS Letters 221: 249-252
(1987)
296. Wang S. M., Sun M. C. and Jeng C. J.: Location of
the C-terminus of titin at the Z-line region in the sarcomere. Biochem. biophys. Res. Commun. 176:
189-193 (1991)
297. Ward S. et al.: Genomic organizations of major sperm
protein genes and pseudogenes in the nematode Caenorhabditis elegans. J. mol. BioI. 199: 1-13 (1988)
298. Wasenius V. M. et al.: a-Actinin and spectrin have
common structural domains. FEBS Letters 221:
73-76 (1987)
299. Watabe S. and Hartshorne D. J.: Paramyosin and the
catch mechanism. Compo Biochem. Physiol. Pt. B 96:
639-646 (1990)
300. Weber K., Plessmann U. and Ulrich w.: Cytoplasmic
intermediate filament proteins of invertebrates are
closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization
of two muscle proteins of a nematode. Embo J. 8:
3221-27 (1989)
301. Weeds A. G. et al.: Preparation and characteriziation
of pig plasma and platelet gelsolins. Eur. J. Biochem.
161: 69-76 (1986)
References
375
302. Weller P. A. et al.: Complete sequence of human vinculin and assignment of the gene to chromosome 10.
Proc. Nat. Acad. Sci. USA 87: 5667-71 (1990)
303. Wesseling J. G. et al.: Nucleotide sequence and
expression of a ~-tubulin-encoding gene from Plasmodium falciparum, a malarial parasite of man. Gene
83: 301-309 (1989)
304. Whitbread L. A., Gregg K. and Rogers G. E.: The
structure and expression of a gene encoding chick
claw keratin. Gene 101: 223-229 (1991)
305. Wiche G.: High-Mt microtubule-associated proteins:
properties and functions. Biochem. J. 259: 1-12 (1989)
306. Wilson P. W. et al.: Structure of chick chromosomal
genes for calbindin and calretinin. J. mol. BioI. 200:
615-625 (1988)
307. Winder S. J. and Walsh M. P.: Smooth muscle calponino Inhibition of actomyosin MgATPase and regulation by phosphorylation. J. BioI. Chern. 265:
10148-55 (1990)
308. Winkelmann J. C. et al.: Full-length sequence of the
cDNA for human erythroid ~-spectrin. J. BioI.
Chern. 265: 11827-32 (1990)
309. Winrow M. A. and Sodja A.: Initial characterization
of several actin genes in the parasitic nematode,
Ascaris suum. Biochem. biophys. Res. Commun.
178: 578-585 (1991)
310. Wistow G. J. and Piatigorsky J.: Gene conversion
and splice-site slippage in the argininosuccinate lyases
delta-crystallins of the duck lens: Members of an
enzyme superfamily. Gene 96: 263-270 (1990)
311. Wistow G., Anderson A. and Piatigorsky J.: Evidence for neutral and selective processes in the recruitment of enzyme-crystallins in avian lenses. Proc. Nat.
Acad. Sci. USA 87: 6277-80 (1990)
312. Wistow G. and Kim H.: Lens protein expression in
mammals. Taxon-specificity and the recruitment of
crystallins. J. mol. Evol. 32: 262-269 (1991)
313. Wohlfarth-Bottermann K. E. (ed.): Nature and function of cytoskeletal proteins in motility and transport.
G. Fischer, Stuttgart 1987
314. Xiang M. et al.: Tandem duplication and divergence
of a sea urchin protein belonging to the troponin C
superfamily. J. BioI. Chern. 263: 17173-80 (1988)
315. Yaffe D. et al.: Highly conserved sequences in the 3'
untranslated region of mRNAs coding for homologous proteins in distantly related species. Nucleic
Acids Res. 13: 3723-37 (1985)
316. Yamanaka M. K. et al.: Structure and expression of
the Drosophila calmodulin gene. Nucleic Acids Res.
15: 3335-48 (1987)
317. Yazaki P. J. et al.: Calsequestrin, an intracellular
calcium-binding protein of skeletal muscle sarcoplasmic reticulum, is homologous to aspartactin, a
putative laminin-binding protein of the extracellular
matrix. Biochem. biophys. Res. Commun. 166:
898-903 (1990)
318. Yazawa M. et al.: The amino acid sequence of the Tetrahymena calmodulin which specifically interacts with
guanylate cyclase. Biochem. biophys. Res. Commun.
99: 1051-57 (1981)
319. Zarain-Herzberg A., Fliegel L. and MacLennan D.
H.: Structure of the rabbit fast-twitch skeletal muscle
calsequestrin gene. J. BioI. Chern. 263: 4807-12
(1988)
320. Zehner Z. E. et al.: The chicken vimentin gene. Nucleotide sequence, regulatory elements, and comparison of
the hamster gene. J. bioI. Chern. 262: 8112-20 (1987)