dynamin reveals homology with a new family of GTPbinding proteins. Nature 347: 256-261 (1990)
206. Ohshima S. et al.: Generation of multiple troponin T
isoforms is a common feature of the muscles in various chordate animals. Compo Biochem. Physiol. Pt.
B 90: 779-784 (1988)
207. Ojima T. and Nishita K.: Troponin from akazara scallop striated muscles. J. bioI. Chern. 261: 16749-54
(1986)
208. Okaimatsuo Y. et al.: A novel myosin heavy chain isoform in the vascular smooth muscle. Biochem. biophys. Res. Commun. 176: 1365-70 (1991)
209. Opperman L. and Ross E P.: The adult fruit bat
(Rousettus aegyptiacus) expresses only calbindinD9K (vitamin-D-dependent calcium-binding protein)
in its kidney. Compo Biochem. Physiol. Pt. B 97:
295-299 (1990)
210. Padan R. et al.: Isolation an characterization of the
Drosophila nuclear envelope otefin cDNA. J. BioI.
Chern. 265: 1808-13 (1990)
211. Palmisano W. A. and Henzl M. T.: Partial nucleotide
sequence of the parvalbumin from chicken thymus
designated "avian thymus hormone". Biochem. biophys. Res. Commun. 167: 1286-93 (1990)
212. Pankov R. G. et al.: Vertebrate liver cytokeratins: a
comparative study. Biochem. cell. BioI. 65: 547-557
(1987)
213. Parmentier M., Lawson D. E. M. and Vassart G.:
Human 27-kDa calbindin complementary DNA
sequence - Evolutionary and functional implications.
Eur. J. Biochem. 170: 207-215 (1987)
214. Parry D. A. D., Conway J. E and Steiner P. M.:
Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins. Biochem. J. 238: 305-308 (1986)
215. Pearlstone J. R., Carpenter M. R. and Smillie L. B.:
Amino acid sequence of rabbit cardiac troponin T. J.
bioI. Chern. 261: 16795-810 (1986)
216. Pegues J. C. and Friedberg E: Multiple messenger
RNAs encoding human calmodulin. Biochem. biophys. Res. Commun. 172: 1145-49 (1990)
217. Perret C., Lomri N. and Thomasset M.: Evolution of
the EF-hand calcium-binding protein family: Evidence for exon shuffling and intron insertion. J. mol.
Evol. 27: 351-364 (1988)
218. Peter B. et al.: Mouse cytoskeletal gamma-actin:
Analysis and implications of the structure of cloned
cDNA and processed pseudogenes. J. mol. BioI. 203:
665-675 (1988)
219. Peter M. et al.: Cloning and sequencing of cDNAclones encoding chicken lamins A and Bl and comparison of the primary structures of vertebrate A- and Btype lamins. J. mol. BioI. 208: 393-404 (1989)
220. Pette D.: Metabolic heterogeneity of muscle fibers. J.
expo BioI. 115: 179-189 (1985)
221. Phillips M. A. et al.: Primary structure of keratinocyte transglutaminase. Proc. Nat. Acad. Sci. USA 87:
9333-37 (1990)
222. Phillips S. B. et al.: The pancornulins: a group of
basic low molecular weight proteins in mammalian
epidermis and epithelium that may function as cornified envelope precursors. Compo Biochem. Physiol.
Pt. B 95: 781-788 (1990)
223. Pochet R., Lawson D. E. M. and Heizmann C. W.
(eds.): Calcium binding proteins in normal and transformed cells. Plenum, New York 1990
224. Pollard T. D. and Cooper J. A.: Actin and actinReferences
373
binding proteins. A critical evaluation of mechanisms
and functions. Annual Rev. Biochem. 55: 987-1035
(1986)
225. Ponnambalam S. et al.: Conservation and diversity in
families of coated vesicle adaptins. J. BioI. Chern.
265: 4814-20 (1990)
226. Powell B. C. et al.: Clustered arrangement of keratin
intermediate filament genes. Proc. Nat. Acad. Sci.
USA 83: 5048-52 (1986)
227. Pratt L. E and Cleveland D. w.: A survey of the
a-tubulin gene family in chicken: unexpected
sequence heterogeneity in the polypeptides encoded
by five expressed genes. Embo J. 7: 931-940 (1988)
228. Presland R. B., Whitbread L. A. and Rogers G. E.:
Avian keratin genes. II. Chromosomal arrangement
and close linkage of three gene families. J. mol. BioI.
209: 561-576 (1989)
229. Price G. J. et al.: Primary sequence and domain
structure of chicken vinculin. Biochem. J. 259:
453-461 (1989)
230. Ramaekers E et al.: Classification of rat lens
crystallins and identification of proteins encoded by
rat lens mRNA. Eur. J. Biochem. 128: 503-508
(1982)
231. Rearden A. et al.: Evolution of the glycophorin gene
family in the hominoid primates. Biochem. Genet.
28: 209-222 (1990)
232. Rees D. J. G. et al.: Sequence and domain structure
of talin. Nature 347: 685-688 (1990)
233. Reeves S. A. et al.: Molecular cloning and primary
structure. of human glial fibrillary acidic protein.
Proc. Nat. Acad. Sci. USA 86: 5178-82 (1989)
234. van Rens G. L. M. et al: Structure of the bovine eye
lens gamma-s-crystallin gene (formerly ~s). Gene 78:
225-233 (1989)
235. Rodgers M. E. et al.: Thermal stability of myosin rod
from various species. Biochemistry 26: 8703-08
(1987)
236. Rogers G. E. et al. (eds.): The biology of wool and
hair. Chapman & Hall, New York 1989
237. Rothnagel J. A. and Steinert P. M.: The structure of
the gene for mouse filaggrin and a comparison of the
repeating units. J. BioI. Chern. 265: 1862-65 (1990)
238. RUegg J. C.: Calcium in muscle activation. A comparative approach, corr. 2nd printing. Springer, Berlin
1988
239. Ruiz-Opazo N. and Nadal-Ginard B.: a-Tropomyosin
gene organization. Alternative splicing of duplicated
isotype-specific exons accounts for the production of
smooth and striated muscle isoforms. J. bioI. Chern.
262: 4755-65 (1987)
240. Sahr K. E. et al.: The complete DNA and polypeptide sequences of human erythroid a-spectrin. J. BioI.
Chern. 265: 4434-43 (1990)
241. Sasaki T., Tanokura M. and Asaoka K.: The complete
amino acid sequence of bullfrog (Rana catesbeiana)
pavalbumin Pi4.97. FEBS Letters 268: 249-251 (1990)
242. Schachat E H., Bronson D. D. and McDonald O. B.:
Heterogenity of contractile proteins. A continuum of
troponin-tropomyosin expression in mammalian skeletal muscle. J. bioI. Chern. 260: 1108-13 (1985)
243. Schaefer W. H. et al.: Amino acid sequence of a novel
calmodulin from Paramecium tetraurelia that contains dimethyllysine in the first domain. J. bioI.
Chern. 262: 1025-29 (1987)
244. Schliwa M.: Cytoskeleton. An introductory survey.
Springer, Wien 1986
206. Ohshima S. et al.: Generation of multiple troponin T
isoforms is a common feature of the muscles in various chordate animals. Compo Biochem. Physiol. Pt.
B 90: 779-784 (1988)
207. Ojima T. and Nishita K.: Troponin from akazara scallop striated muscles. J. bioI. Chern. 261: 16749-54
(1986)
208. Okaimatsuo Y. et al.: A novel myosin heavy chain isoform in the vascular smooth muscle. Biochem. biophys. Res. Commun. 176: 1365-70 (1991)
209. Opperman L. and Ross E P.: The adult fruit bat
(Rousettus aegyptiacus) expresses only calbindinD9K (vitamin-D-dependent calcium-binding protein)
in its kidney. Compo Biochem. Physiol. Pt. B 97:
295-299 (1990)
210. Padan R. et al.: Isolation an characterization of the
Drosophila nuclear envelope otefin cDNA. J. BioI.
Chern. 265: 1808-13 (1990)
211. Palmisano W. A. and Henzl M. T.: Partial nucleotide
sequence of the parvalbumin from chicken thymus
designated "avian thymus hormone". Biochem. biophys. Res. Commun. 167: 1286-93 (1990)
212. Pankov R. G. et al.: Vertebrate liver cytokeratins: a
comparative study. Biochem. cell. BioI. 65: 547-557
(1987)
213. Parmentier M., Lawson D. E. M. and Vassart G.:
Human 27-kDa calbindin complementary DNA
sequence - Evolutionary and functional implications.
Eur. J. Biochem. 170: 207-215 (1987)
214. Parry D. A. D., Conway J. E and Steiner P. M.:
Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins. Biochem. J. 238: 305-308 (1986)
215. Pearlstone J. R., Carpenter M. R. and Smillie L. B.:
Amino acid sequence of rabbit cardiac troponin T. J.
bioI. Chern. 261: 16795-810 (1986)
216. Pegues J. C. and Friedberg E: Multiple messenger
RNAs encoding human calmodulin. Biochem. biophys. Res. Commun. 172: 1145-49 (1990)
217. Perret C., Lomri N. and Thomasset M.: Evolution of
the EF-hand calcium-binding protein family: Evidence for exon shuffling and intron insertion. J. mol.
Evol. 27: 351-364 (1988)
218. Peter B. et al.: Mouse cytoskeletal gamma-actin:
Analysis and implications of the structure of cloned
cDNA and processed pseudogenes. J. mol. BioI. 203:
665-675 (1988)
219. Peter M. et al.: Cloning and sequencing of cDNAclones encoding chicken lamins A and Bl and comparison of the primary structures of vertebrate A- and Btype lamins. J. mol. BioI. 208: 393-404 (1989)
220. Pette D.: Metabolic heterogeneity of muscle fibers. J.
expo BioI. 115: 179-189 (1985)
221. Phillips M. A. et al.: Primary structure of keratinocyte transglutaminase. Proc. Nat. Acad. Sci. USA 87:
9333-37 (1990)
222. Phillips S. B. et al.: The pancornulins: a group of
basic low molecular weight proteins in mammalian
epidermis and epithelium that may function as cornified envelope precursors. Compo Biochem. Physiol.
Pt. B 95: 781-788 (1990)
223. Pochet R., Lawson D. E. M. and Heizmann C. W.
(eds.): Calcium binding proteins in normal and transformed cells. Plenum, New York 1990
224. Pollard T. D. and Cooper J. A.: Actin and actinReferences
373
binding proteins. A critical evaluation of mechanisms
and functions. Annual Rev. Biochem. 55: 987-1035
(1986)
225. Ponnambalam S. et al.: Conservation and diversity in
families of coated vesicle adaptins. J. BioI. Chern.
265: 4814-20 (1990)
226. Powell B. C. et al.: Clustered arrangement of keratin
intermediate filament genes. Proc. Nat. Acad. Sci.
USA 83: 5048-52 (1986)
227. Pratt L. E and Cleveland D. w.: A survey of the
a-tubulin gene family in chicken: unexpected
sequence heterogeneity in the polypeptides encoded
by five expressed genes. Embo J. 7: 931-940 (1988)
228. Presland R. B., Whitbread L. A. and Rogers G. E.:
Avian keratin genes. II. Chromosomal arrangement
and close linkage of three gene families. J. mol. BioI.
209: 561-576 (1989)
229. Price G. J. et al.: Primary sequence and domain
structure of chicken vinculin. Biochem. J. 259:
453-461 (1989)
230. Ramaekers E et al.: Classification of rat lens
crystallins and identification of proteins encoded by
rat lens mRNA. Eur. J. Biochem. 128: 503-508
(1982)
231. Rearden A. et al.: Evolution of the glycophorin gene
family in the hominoid primates. Biochem. Genet.
28: 209-222 (1990)
232. Rees D. J. G. et al.: Sequence and domain structure
of talin. Nature 347: 685-688 (1990)
233. Reeves S. A. et al.: Molecular cloning and primary
structure. of human glial fibrillary acidic protein.
Proc. Nat. Acad. Sci. USA 86: 5178-82 (1989)
234. van Rens G. L. M. et al: Structure of the bovine eye
lens gamma-s-crystallin gene (formerly ~s). Gene 78:
225-233 (1989)
235. Rodgers M. E. et al.: Thermal stability of myosin rod
from various species. Biochemistry 26: 8703-08
(1987)
236. Rogers G. E. et al. (eds.): The biology of wool and
hair. Chapman & Hall, New York 1989
237. Rothnagel J. A. and Steinert P. M.: The structure of
the gene for mouse filaggrin and a comparison of the
repeating units. J. BioI. Chern. 265: 1862-65 (1990)
238. RUegg J. C.: Calcium in muscle activation. A comparative approach, corr. 2nd printing. Springer, Berlin
1988
239. Ruiz-Opazo N. and Nadal-Ginard B.: a-Tropomyosin
gene organization. Alternative splicing of duplicated
isotype-specific exons accounts for the production of
smooth and striated muscle isoforms. J. bioI. Chern.
262: 4755-65 (1987)
240. Sahr K. E. et al.: The complete DNA and polypeptide sequences of human erythroid a-spectrin. J. BioI.
Chern. 265: 4434-43 (1990)
241. Sasaki T., Tanokura M. and Asaoka K.: The complete
amino acid sequence of bullfrog (Rana catesbeiana)
pavalbumin Pi4.97. FEBS Letters 268: 249-251 (1990)
242. Schachat E H., Bronson D. D. and McDonald O. B.:
Heterogenity of contractile proteins. A continuum of
troponin-tropomyosin expression in mammalian skeletal muscle. J. bioI. Chern. 260: 1108-13 (1985)
243. Schaefer W. H. et al.: Amino acid sequence of a novel
calmodulin from Paramecium tetraurelia that contains dimethyllysine in the first domain. J. bioI.
Chern. 262: 1025-29 (1987)
244. Schliwa M.: Cytoskeleton. An introductory survey.
Springer, Wien 1986