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Truncation mutagenesis of the non - Helical carboxy-terminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly
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Rogers KR, Eckelt A, Nimmrich V, Janssen K-P, Schliwa M, Herrmann H, Franke WW. Truncation mutagenesis of the non - helical carboxy-terminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur J Cell Biol. 66:1995;136-150.
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(1995)
Eur J Cell Biol
, vol.66
, pp. 136-150
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Rogers, K.R.1
Eckelt, A.2
Nimmrich, V.3
Janssen K-P4
Schliwa, M.5
Herrmann, H.6
Franke, W.W.7
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49
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0031578625
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A splice site mutation in the gene of the human type I hair keratin results in the expression of tailless keratin isoform
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of special interest. The generation of a tail-less hair keratin as a consequence of a splice site point mutation is demonstrated. The recombinant hair keratins, hHa1 (and also the tail-less hHa 1-t) and hHb3, form IFs in vitro, although conditions known to be optimal for type III IF proteins rather than for cytokeratins (i.e. 160 mM NaCl versus no salt) had to be employed. With cytokeratin 8 as its basic assembly partner, conventional cytokeratin assembly conditions (i.e. 5 to 50 mM Tris-HCl without NaCl) were sufficient for hHa1 to form smooth-surfaced IFs. This again indicates that different IF proteins may respond quite uniquely to certain ionic conditions [39,50].
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Winter H, Hofmann I, Langbein L, Rogers MA, Schweizer J. A splice site mutation in the gene of the human type I hair keratin results in the expression of tailless keratin isoform. of special interest J Biol Chem. 272:1997;32345-32352 The generation of a tail-less hair keratin as a consequence of a splice site point mutation is demonstrated. The recombinant hair keratins, hHa1 (and also the tail-less hHa 1-t) and hHb3, form IFs in vitro, although conditions known to be optimal for type III IF proteins rather than for cytokeratins (i.e. 160 mM NaCl versus no salt) had to be employed. With cytokeratin 8 as its basic assembly partner, conventional cytokeratin assembly conditions (i.e. 5 to 50 mM Tris-HCl without NaCl) were sufficient for hHa1 to form smooth-surfaced IFs. This again indicates that different IF proteins may respond quite uniquely to certain ionic conditions [39,50].
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(1997)
J Biol Chem
, vol.272
, pp. 32345-32352
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Winter, H.1
Hofmann, I.2
Langbein, L.3
Rogers, M.A.4
Schweizer, J.5
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50
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0031045209
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Heterotypic interactions and filament assembly of type I and type II cytokeratins in vitro: Viscometry and determinations of relative affinities
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of special interest. A panel of recombinant cytokeratins was employed to demonstrate, using surface plasmon resonance, the varying relative affinities of the basic cytokeratin 8 or various acidic cytokeratins. In parallel, viscometric analysis was performed. Interestingly, the weakest binding partner, cytokeratin 20, yields the highest viscosity when co-assembled with cytokeratin 8 at low ionic strength. The influence of increasing ionic strength on assembly performance is completely different for the various cytokeratin pairs.
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Hofmann I, Franke WW. Heterotypic interactions and filament assembly of type I and type II cytokeratins in vitro: viscometry and determinations of relative affinities. of special interest Eur J Cell Biol. 72:1997;122-132 A panel of recombinant cytokeratins was employed to demonstrate, using surface plasmon resonance, the varying relative affinities of the basic cytokeratin 8 or various acidic cytokeratins. In parallel, viscometric analysis was performed. Interestingly, the weakest binding partner, cytokeratin 20, yields the highest viscosity when co-assembled with cytokeratin 8 at low ionic strength. The influence of increasing ionic strength on assembly performance is completely different for the various cytokeratin pairs.
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(1997)
Eur J Cell Biol
, vol.72
, pp. 122-132
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Hofmann, I.1
Franke, W.W.2
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51
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0001051091
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Structure, assembly and dynamics of intermediate filaments
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H. Herrmann, Harris J.R. New York: Plenum Press. [Harris JR (series editor): Subcellular Biochemistry, vol 31.]
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Herrmann H, Aebi U. Structure, assembly and dynamics of intermediate filaments. Herrmann H, Harris JR. Intermediate Filaments. 1998;Plenum Press, New York. [Harris JR (series editor): Subcellular Biochemistry, vol 31.].
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(1998)
Intermediate Filaments
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Herrmann, H.1
Aebi, U.2
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52
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0029940902
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Vimentin in a cold-water fish, the rainbow trout: Highly conserved primary structure but unique assembly properties
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Herrmann H, Münick D, Brettel M, Fouquet B, Markl J. Vimentin in a cold-water fish, the rainbow trout: highly conserved primary structure but unique assembly properties. J Cell Sci. 109:1996;569-578.
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(1996)
J Cell Sci
, vol.109
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Herrmann, H.1
Münick, D.2
Brettel, M.3
Fouquet, B.4
Markl, J.5
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53
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0030024023
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Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells
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Goulielmos G, Gounari F, Remington S, Müller S, Hänet M, Aebi U, Georgatos SD. Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells. J Cell Biol. 132:1996;643-655.
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(1996)
J Cell Biol
, vol.132
, pp. 643-655
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Goulielmos, G.1
Gounari, F.2
Remington, S.3
Müller, S.4
Hänet, M.5
Aebi, U.6
Georgatos, S.D.7
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54
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0030717391
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To bead or not to bead? Lens-specific intermediate filaments revisited
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of special interest. The peculiar assembly characteristics of the somehow 'odd' prominent representatives of the lens cytoskeleton, phakinin and filensin, are discussed. These proteins - true IF proteins without a clear 'class' membership - constitute a unique structure previously referred to as a 'beaded-chain' filament. See also Georgatos and co-workers [53].
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Georgatos SD, Gounari F, Goulielmos G, Aebi U. To bead or not to bead? Lens-specific intermediate filaments revisited. of special interest J Cell Sci. 110:1997;2629-2634 The peculiar assembly characteristics of the somehow 'odd' prominent representatives of the lens cytoskeleton, phakinin and filensin, are discussed. These proteins - true IF proteins without a clear 'class' membership - constitute a unique structure previously referred to as a 'beaded-chain' filament. See also Georgatos and co-workers [53].
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(1997)
J Cell Sci
, vol.110
, pp. 2629-2634
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Georgatos, S.D.1
Gounari, F.2
Goulielmos, G.3
Aebi, U.4
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55
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0001481064
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Dynamic property of intermediate filaments: Regulation by phosphorylation
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Inagaki M, Matsuoka Y, Tsujimura K, Ando S, Tokui T, Takahashi T, Inagaki N. Dynamic property of intermediate filaments: regulation by phosphorylation. Bioessays. 18:1996;481-487.
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(1996)
Bioessays
, vol.18
, pp. 481-487
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Inagaki, M.1
Matsuoka, Y.2
Tsujimura, K.3
Ando, S.4
Tokui, T.5
Takahashi, T.6
Inagaki, N.7
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56
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0028360655
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Mitotic arrest with anti-microtubule agents or okadaic acid is associated with increased glycoprotein terminal GlcNAc's
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Chou C-F, Omary MB. Mitotic arrest with anti-microtubule agents or okadaic acid is associated with increased glycoprotein terminal GlcNAc's. J Cell Sci. 107:1994;1833-1843.
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(1994)
J Cell Sci
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, pp. 1833-1843
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Chou C-F1
Omary, M.B.2
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57
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0030588237
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Characterization of ADP-ribosylation sites on desmin and restoration of desmin intermediate filament assembly by de-ADP-ribosylation
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Zhou H, Huiatt TW, Robson RM, Sernett SW, Graves DJ. Characterization of ADP-ribosylation sites on desmin and restoration of desmin intermediate filament assembly by de-ADP-ribosylation. Arch Biochem Biophys. 334:1996;214-222.
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Arch Biochem Biophys
, vol.334
, pp. 214-222
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Zhou, H.1
Huiatt, T.W.2
Robson, R.M.3
Sernett, S.W.4
Graves, D.J.5
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58
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0032006027
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Intermediate filaments and their associated proteins: Multiple dynamic personalities
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of outstanding interest. A comprehensive and up to date review on the importance of specific cytoskeletal cross-linking factors for the integration of the various IF systems in to their respective cell-type-specific cytoskeletons. Besides this conceptual outline, a thorough account of the importance of various IF proteins in new human disorders is presented.
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Houseweart MK, Cleveland DW. Intermediate filaments and their associated proteins: multiple dynamic personalities. of outstanding interest Curr Opin Cell Biol. 10:1998;93-101 A comprehensive and up to date review on the importance of specific cytoskeletal cross-linking factors for the integration of the various IF systems in to their respective cell-type-specific cytoskeletons. Besides this conceptual outline, a thorough account of the importance of various IF proteins in new human disorders is presented.
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(1998)
Curr Opin Cell Biol
, vol.10
, pp. 93-101
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Houseweart, M.K.1
Cleveland, D.W.2
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59
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0030915589
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Neurofilaments and motor neuron disease
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of outstanding interest. Studies of transgenic mice expressing various neurofilament polypeptides reveal pathological conditions resembling those found in motor neuron diseases. Evidence is presented for the fact that mutations in superoxide dismutase and the genesis of neurofilament accumulations are connected and instrumental in the pathogenesis of some neurological disorders such as amyotrophic lateral sclerosis.
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Julien J-P. Neurofilaments and motor neuron disease. of outstanding interest Trends Cell Biol. 7:1997;243-249 Studies of transgenic mice expressing various neurofilament polypeptides reveal pathological conditions resembling those found in motor neuron diseases. Evidence is presented for the fact that mutations in superoxide dismutase and the genesis of neurofilament accumulations are connected and instrumental in the pathogenesis of some neurological disorders such as amyotrophic lateral sclerosis.
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(1997)
Trends Cell Biol
, vol.7
, pp. 243-249
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Julien J-P1
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60
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0030198631
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Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels
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of special interest. Using oxidative cross-linking of the single cysteine of vimentin, as well as recombinant vimentin that is essentially cysteine-free or has newly introduced cysteines, the interaction of individual molecules within dimers and tetramers was followed. In particular, the extremely rapid exchange of vimentin and desmin within dimers at 5 M urea demonstrated the very high affinity of both proteins for one another at the coiled-coil level, regardless of considerable primary sequence differences.
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Rogers KR, Herrmann H, Franke WW. Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels. of special interest J Struct Biol. 117:1996;55-69 Using oxidative cross-linking of the single cysteine of vimentin, as well as recombinant vimentin that is essentially cysteine-free or has newly introduced cysteines, the interaction of individual molecules within dimers and tetramers was followed. In particular, the extremely rapid exchange of vimentin and desmin within dimers at 5 M urea demonstrated the very high affinity of both proteins for one another at the coiled-coil level, regardless of considerable primary sequence differences.
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(1996)
J Struct Biol
, vol.117
, pp. 55-69
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Rogers, K.R.1
Herrmann, H.2
Franke, W.W.3
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