Bibliography
Hanukoglu, I., & Fuchs, E. (1986). STRUCTURAL DIVERSITY AND EVOLUTION OF INTERMEDIATE FILAMENT PROTEINS11Our work reviewed here was supported by a U.S. National Institutes of Health grant. I. H. was the recipient of a U.S. National Cancer Institute National Research Service Award. E. F. is the recipient of a National Institutes of Health Career Development Award and a Presidential Young Investigator Award. Evolutionary Processes and Theory, 69â98.
References
87
Referenced
5
10.1016/0014-5793(84)80468-8
/ FEBS Lett. / Control of intermediate filament protein synthesis by cell-cell interaction and cell configuration by Ben-Zeev (1984){'key': '10.1016/B978-0-12-398760-0.50008-0_bib2', 'first-page': '45', 'article-title': 'Prediction of the secondary structure of proteins from their amino acid sequence', 'volume': '47', 'author': 'Chou', 'year': '1978', 'journal-title': 'Adv. Enzymol.'}
/ Adv. Enzymol. / Prediction of the secondary structure of proteins from their amino acid sequence by Chou (1978)10.1016/S0006-3495(79)85259-5
/ Biophys. J. / Prediction of β-turns by Chou (1979)10.1126/science.6344214
/ Science / Splice junctions: Association with variation in protein structure by Craik (1983)10.1016/0092-8674(83)90174-5
/ Cell / Tissue-specific expression of two mRNA species transcribed from a single vimentin gene by Capetanaki (1983)10.1016/S0021-9258(18)99539-6
/ J. Biol. Chem. / The preparation and properties of a helix-rich fraction obtained by partial proteolysis of low sulfur S-carboxymethyl-kerateine from wool by Crewther (1967)10.1042/bj1730365
/ Biochem. J. / Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A by Crewther (1978)- Crewther, W. G., Dowling, L. M., and Inglis, A. S. (1980). Amino acid sequence data from a microfibrillar protein of α-keratin. In “The Structure and Chemical Reactions of Keratins,” Vol. 2, pp. 79–91.
10.1107/S0365110X53001964
/ Acta Cryst. / The packing of α-helices: simple coiled-coils by Crick (1953)10.1007/BF01121573
/ Biosci. Rep. / Structural homology between hard α-keratin and the intermediate filament proteins desmin and vimentin by Dowling (1983)10.1083/jcb.98.4.1388
/ J. Cell Biol. / Classification of epidermal keratins according to their immunoreactivity, isoelectric point and mode of expression by Eichner (1984)10.1042/bj1730387
/ Biochem. J. / Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A: Statistical analysis by Elleman (1978)10.1101/SQB.1982.046.01.041
/ Cold Spring Harbor Symp. Quant. Biol. / Differentiation-related patterns of expression of protein of intermediate-size filament in tissues and cultured cells by Franke (1982)10.1073/pnas.80.23.7113
/ Proc. Natl. Acad. Sci. USA / Protein complexes of intermediate-sized filaments: melting of cytokeratin complexes in urea reveals different polypeptide separation characteristics by Franke (1983){'key': '10.1016/B978-0-12-398760-0.50008-0_bib15', 'series-title': '“Keratins: Their Composition, Structure and Biosynthesis', 'author': 'Fraser', 'year': '1972'}
/ “Keratins: Their Composition, Structure and Biosynthesis by Fraser (1972)10.1016/S0022-2836(76)80129-5
/ J. Mol. Biol. / Structure of the α-keratin microfibril by Fraser (1976)10.1016/0092-8674(81)90362-7
/ Cell / Two distinct classes of keratin genes and their evolutionary significance by Fuchs (1982)10.1073/pnas.80.19.5857
/ Proc. Natl. Acad. Sci. USA / Type I and type II keratins have evolved from lower eukaryotes to form the epidermal intermediate filaments in mammalian skin by Fuchs (1983)-
Fuchs, E., and Hanukoglu, I. (1986). Epidermal α-keratins: Structural diversity and changes during tissue differentiation. In “The Biology of the Integument” (in press).
(
10.1007/978-3-662-00989-5_32
) 10.1073/pnas.76.8.3894
/ Proc. Natl. Acad. Sci. USA / Coexistence of desmin and the fibroblastic intermediate filament subunit in muscle and nonmuscle cells: Identification and comparative peptide analysis by Gard (1983)10.1016/0022-2836(78)90297-8
/ J. Mol. Biol. / Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins by Garnier (1978)10.1002/j.1460-2075.1982.tb01368.x
/ EMBO J. / The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins by Geisler (1982)10.1016/0092-8674(82)90033-2
/ Cell / Protein chemical characterization of three structurally distinct domains along the protofilament unit of desmin 10nm filaments by Geisler (1982)10.1002/j.1460-2075.1985.tb02317.x
/ EMBO J. / Hybrid character of a large neurofilament protein (NF-M): intermediate filament type sequence followed by a long and acidic carboxy-terminal extension by Geisler (1984)10.1002/j.1460-2075.1985.tb02317.x
/ EMBO J. / Protein-chemical characterization of NF-H, the largest mammalian neurofilament component; intermediate filament-type sequences followed by a unique carboxy terminal extensions by Geisler (1985)10.1073/pnas.80.7.1964
/ Proc. Natl. Acad. Sci. USA / Modular structural units, exons, and function in chicken lysozyme by Go (1983)10.1042/bj1730373
/ Biochem. J. / Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A by Gough (1978)10.1126/science.6346488
/ Science / Expression of major neurofilament subunit in chicken erythrocytes by Granger (1983)10.1042/bj2090587
/ Biochem. J. / Structural studies on the microfibrillar proteins of wool by Gruen (1983)10.1016/0092-8674(82)90424-X
/ Cell / The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins by Hanukoglu (1982)10.1016/0092-8674(83)90034-X
/ Cell / The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins by Hanukoglu (1983)10.1016/0022-2836(83)90117-1
/ J. Mol. Biol. / Complementary DNA sequence of a human cytoplasmic actin by Hanukoglu (1983)10.1083/jcb.98.4.1523
/ J. Cell Biol. / Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton by Hirokawa (1984)10.1016/0022-2836(82)90444-2
/ J. Mol. Biol. / A periodic ultrastructure in intermediate filaments by Henderson (1982)10.1002/j.1460-2075.1984.tb01966.x
/ EMBO J. / Amino acid sequence of the carboxy-terminal part of an acidic type I cytokeratin of molecular weight 51000 from Xenopus laevis epidermis as predicted from the cDNA sequence by Hoffman (1984){'key': '10.1016/B978-0-12-398760-0.50008-0_bib36', 'first-page': '552', 'article-title': 'Expression of vimentin and cytokeratin types of intermediate filament proteins in developing and adult human kidneys', 'volume': '50', 'author': 'Holthofer', 'year': '1984', 'journal-title': 'Lab. Invest.'}
/ Lab. Invest. / Expression of vimentin and cytokeratin types of intermediate filament proteins in developing and adult human kidneys by Holthofer (1984)10.1007/BF02100227
/ J. Mol. Evol. / Accepted mutations in a gene family: Evolutionary diversification of duplicated DNA by Jones (1982)10.1016/0005-2795(75)90342-6
/ Biochim. Biophys. Acta. / The isolation and characterization of α-keratin microfibrils by Jones (1975)10.1016/0022-2836(84)90468-6
/ J. Mol. Biol. / Identification of two types of keratin polypeptides within the acidic cytokeratin subfamily I by Jorcano (1984)10.1083/jcb.32.1.227
/ J. Cell. Biol. / Periodic repeat units of epithelial cell tonofilaments by Kallman (1967)10.1128/MCB.3.4.495
/ Mol. Cell. Biol. / Tissue specificity of epithelial keratins: Differential expression of mRNAs from two multigene families by Kim (1983)10.1083/jcb.99.5.1872
/ J. Cell Biol. / Expression of unusually large keratins during terminal differentiation: Balance of type I and type II keratins is not disrupted by Kim (1984)10.1073/pnas.81.14.4280
/ Proc. Natl. Acad. Sci. USA / Differences in keratin synthesis between normal epithelial cells and squamous cell carcinomas are mediated by vitamin A by Kim (1984)10.1146/annurev.bi.51.070182.001251
/ Ann. Rev. Biochem. / Intermediate filaments; A chemically heterogeneous, developmentally regulated class of proteins by Lazarides (1982)10.1038/303701a0
/ Nature / Co-expression of vimentin and cytokeratins in parietal endoderm cells of early mouse embryo by Lane (1983)10.1038/264377a0
/ Nature / Organisation of the polypeptide chains in mammalian keratin by Lee (1976)10.1002/j.1460-2075.1984.tb02290.x
/ EMBO J. / Characterization of bovine keratin genes: similarities of exon patterns in genes coding for different keratins by Lehnert (1984)10.1073/pnas.81.9.2743
/ Proc. Natl. Acad. Sci. USA / Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: structural conservation of intermediate filaments by Lewis (1984)10.1016/0092-8674(85)90311-3
/ Cell / Intron/exon structure of the chicken pyruvate kinase gene by Lonberg (1985)10.1016/0141-8130(83)90058-2
/ Int. J. Biol. Macromol. / The N-terminal domain of desmin is not involved in intermediate filament formation: evidence from thrombic digestion studies by Lu (1983)10.1016/0092-8674(84)90456-2
/ Cell / Remarkable conservation of structure among intermediate filament genes by Marchuk (1984)10.1073/pnas.82.6.1609
/ Proc. Natl. Acad. Sci. USA / Complete sequence of a gene encoding a human type I keratin: Sequences homologous to enhancer elements in the regulatory region of the gene by Marchuk (1985)10.1126/science.1138367
/ Science / The evolution of a gene by Markert (1975)10.1016/0022-2836(78)90163-8
/ J. Mol. Biol. / Coiled coil formation and sequence regularities in the helical regions of α-keratin by McLachlan (1978)10.1016/0022-2836(82)90396-5
/ J. Mol. Biol. / Periodic charge distribution in the intermediate filament proteins desmin and vimentin by McLachlan (1982)10.1083/jcb.94.3.592
/ J. Cell. Biol. / Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments by Milam (1982)10.1016/0092-8674(82)90400-7
/ Cell / The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells by Moll (1982)10.1016/0022-2836(77)90153-X
/ J. Mol. Biol. / Structure of α-keratin: Structural implication of the amino acid sequences of the type I and type II chain segments by Parry (1977)10.1038/171059a0
/ Nature / Compound helical configurations of polypeptide chains: structure of proteins of the α-keratin type by Pauling (1953)10.1016/0092-8674(83)90224-6
/ Cell / The structure of the vimentin gene by Quax (1983)10.1073/pnas.81.19.5970
/ Proc. Natl. Acad. Sci. USA / Intermediate filament cDNAs from BHK-21 cells: demonstration of distinct genes for desmin and vimentin in all vertebrate classes by Quax (1984)10.1073/pnas.79.11.3452
/ Proc. Natl. Acad. Sci. USA / Heteropolymer filaments of vimentin and desmin in vascular smooth muscle tissue and cultured baby hamster kidney cells demonstrated by chemical crosslinking by Quinlan (1982)10.1016/0022-2836(84)90149-9
/ J. Mol. Biol. / Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells by Quinlan (1984)10.1073/pnas.80.4.1043
/ Proc. Natl. Acad. Sci. USA / Silkmoth chorion multigene families constitute a superfamily: Comparison of C and B family sequences by Regier (1983)10.1016/0014-4827(82)90227-0
/ Ex. Cell Res. / Occurrence of two different intermediate filament protein in the same filament in situ within a human glioma cell line by Sharp (1982)10.1016/S0021-9258(19)43739-3
/ J. Biol. Chem. / Isolation and characterization of the helical regions of epidermal prekeratin by Skerrow (1973)10.1016/0022-2836(78)90376-5
/ J. Mol. Biol. / Structure of the three-chain unit of the bovine epidermal keratin filaments by Steinert (1978)10.1016/S0022-2836(76)80136-2
/ J. Mol. Biol. / Self-assembly of bovine epidermal keratin filaments in vitro by Steinert (1976)10.1073/pnas.77.8.4534
/ Proc. Natl. Acad. Sci. USA / Intermediate filaments of baby hamster kidney (BHK-21) cells and bovine epidermal keratinocytes have similar ultrastructures and subunit domain structures by Steinert (1980)10.1101/SQB.1982.046.01.043
/ Cold Spring Harbor Symp. Quant. Biol. / Heterogeneity of intermediate filaments assembled in vitro by Steinert (1982)10.1038/302794a0
/ Nature / Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments by Steinert (1983)10.1073/pnas.81.18.5709
/ Proc. Natl. Acad. Sci. USA / The complete cDNA and deduced amino acid sequence of a type II mouse epidermal keratin of 60,000 Da: analysis of sequence differences between type I and type II keratins by Steinert (1984)10.1073/pnas.76.6.2813
/ Proc. Natl. Acad. Sci. USA / Keratin cytoskeletons in epithelial cells of internal organs by Sun (1979)10.1126/science.7209528
/ Science / Vitellogenesis and vitellogenin gene family by Wahli (1981)10.1007/BF00222479
/ Mol. Cell. Biochem. / A monoclonal antibody that detects vimentin-related proteins in invertebrates by Walter (1984)10.1073/pnas.81.7.2102
/ Proc. Natl. Acad. Sci. USA / Identification of glial filament protein and vimentin in the same intermediate filament system in human glioma cells by Wang (1984){'key': '10.1016/B978-0-12-398760-0.50008-0_bib77', 'first-page': '110', 'article-title': 'Antibodies against merokeratin from sheep wool decorate cytokeratin filaments in non-keratinizing epithelial cells', 'volume': '23', 'author': 'Weber', 'year': '1980', 'journal-title': 'Eur. J. Cell. biol.'}
/ Eur. J. Cell. biol. / Antibodies against merokeratin from sheep wool decorate cytokeratin filaments in non-keratinizing epithelial cells by Weber (1980)10.1071/BI9810515
/ Aust. J. Biol. Sci. / Sturctural studies on the microfibrillar proteins of wool: characterization of the α-helix particle produced by chymotryptic digestion by Woods (1983)10.1073/pnas.80.4.911
/ Proc. Natl. Acad. Sci. USA / Characterization of the chicken vimentin gene: single copy gene producing multiple mRNAs by Zehner (1983)10.1007/BF01117063
/ Biosci. Rep. / Partial sequence homologies between cytoskeletal proteins, c-myc, Rous sarcoma virus and adenovirus proteins, transducin, and β- and α- crystallins by Crabbe (1985)10.1016/0092-8674(85)90333-2
/ Cell / A cellular gene encodes scrapie PrP 27–30 protein by Oesch (1985)10.1016/0014-5793(85)80357-4
/ FEBS Lett. / The complete amino acid sequence of the major mammalian neurofilament protein (NF-L) by Geisler (1985)10.1073/pnas.82.7.1896
/ Proc. Natl. Acad. Sci. USA / Structure of a gene for the human epidermal 67-kDa keratin by Johnson (1985)10.1111/j.1432-0436.1984.tb00278.x
/ Differentiation / Amino acid sequence diversity between bovine epidermal cytokeratin polypeptides of the basic (type II) subfamily as determined from cDNA clones by Jorcano (1984)10.1016/S0021-9258(18)88905-0
/ J. Biol. Chem. / Organization of a type I keratin gene by Krieg (1985)10.1016/S0021-9258(18)88900-1
/ J. Biol. Chem. / Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits by Steinert (1985)10.1073/pnas.82.14.4683
/ Proc. Natl. Acad. Sci. USA / The sequence of a type II keratin gene expressed in human skin: Conservation of structure among all intermediate filament genes by Tyner (1985)
Dates
Type | When |
---|---|
Created | 11 years ago (Aug. 15, 2014, 8:02 a.m.) |
Deposited | 3 years, 4 months ago (April 14, 2022, 3:39 p.m.) |
Indexed | 1 week, 5 days ago (Aug. 21, 2025, 12:33 p.m.) |
Issued | 39 years, 8 months ago (Jan. 1, 1986) |
Published | 39 years, 8 months ago (Jan. 1, 1986) |
Published Print | 39 years, 8 months ago (Jan. 1, 1986) |
@inbook{Hanukoglu_1986, title={STRUCTURAL DIVERSITY AND EVOLUTION OF INTERMEDIATE FILAMENT PROTEINS11Our work reviewed here was supported by a U.S. National Institutes of Health grant. I. H. was the recipient of a U.S. National Cancer Institute National Research Service Award. E. F. is the recipient of a National Institutes of Health Career Development Award and a Presidential Young Investigator Award.}, ISBN={9780123987600}, url={http://dx.doi.org/10.1016/b978-0-12-398760-0.50008-0}, DOI={10.1016/b978-0-12-398760-0.50008-0}, booktitle={Evolutionary Processes and Theory}, publisher={Elsevier}, author={Hanukoglu, Israel and Fuchs, Elaine}, year={1986}, pages={69–98} }