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Volumn 325, Issue 1, 2004, Pages 276-280

The NC1 domain of human collagen IV is necessary to initiate triple helix formation

Author keywords

Collagen IV; Triple helix

Indexed keywords

CHIMERIC PROTEIN; COLLAGEN TYPE 4; PROTEIN SUBUNIT; STRUCTURAL PROTEIN;

EID: 7444230417     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.10.034     Document Type: Article
Times cited : (23)

References (19)
  • 1
    • 0015132411 scopus 로고
    • Isolation of a collagen from basement membranes containing three identical-chains
    • N.A. Kefalides Isolation of a collagen from basement membranes containing three identical-chains Biochem. Biophys. Res. Commun. 45 1971 226 234
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 226-234
    • Kefalides, N.A.1
  • 2
    • 0023015217 scopus 로고
    • Structure, development, and molecular pathology of basement membranes
    • R. Timpl, and M. Dziadek Structure, development, and molecular pathology of basement membranes Int. Rev. Exp. Pathol. 29 1986 1 112
    • (1986) Int. Rev. Exp. Pathol. , vol.29 , pp. 1-112
    • Timpl, R.1    Dziadek, M.2
  • 3
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • P.D. Yurchenco, P.S. Amenta, and B.L. Patton Basement membrane assembly, stability and activities observed through a developmental lens Matrix Biol. 22 2004 521 538
    • (2004) Matrix Biol. , vol.22 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 4
    • 0035958849 scopus 로고    scopus 로고
    • The NC1 domain of collagen IV encodes a novel network composed of the alpha 1, alpha 2, alpha 5, and alpha 6 chains in smooth muscle basement membranes
    • D.B. Borza, O. Bondar, Y. Ninomiya, Y. Sado, I. Naito, P. Todd, and B.G. Hudson The NC1 domain of collagen IV encodes a novel network composed of the alpha 1, alpha 2, alpha 5, and alpha 6 chains in smooth muscle basement membranes J. Biol. Chem. 276 2001 28532 28540
    • (2001) J. Biol. Chem. , vol.276 , pp. 28532-28540
    • Borza, D.B.1    Bondar, O.2    Ninomiya, Y.3    Sado, Y.4    Naito, I.5    Todd, P.6    Hudson, B.G.7
  • 5
    • 0028639246 scopus 로고
    • Basement membrane (type IV) collagen
    • K. Kuhn Basement membrane (type IV) collagen Matrix Biol. 14 1995 439 445
    • (1995) Matrix Biol. , vol.14 , pp. 439-445
    • Kuhn, K.1
  • 6
    • 0025904728 scopus 로고
    • The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper
    • J. Engel, and D.J. Prockop The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper Annu. Rev. Biophys. Biophys. Chem. 20 1991 137 152
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 137-152
    • Engel, J.1    Prockop, D.J.2
  • 7
    • 0029834980 scopus 로고    scopus 로고
    • Triple helix formation of procollagen type I can occur at the rough endoplasmic reticulum membrane
    • K. Beck, B.A. Boswell, C.C. Ridgway, and H.P. Bachinger Triple helix formation of procollagen type I can occur at the rough endoplasmic reticulum membrane J. Biol. Chem. 271 1996 21566 21573
    • (1996) J. Biol. Chem. , vol.271 , pp. 21566-21573
    • Beck, K.1    Boswell, B.A.2    Ridgway, C.C.3    Bachinger, H.P.4
  • 10
    • 0024339276 scopus 로고
    • Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix
    • J.M. Davis, B.A. Boswell, and H.P. Bachinger Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix J. Biol. Chem. 264 1989 8956 8962
    • (1989) J. Biol. Chem. , vol.264 , pp. 8956-8962
    • Davis, J.M.1    Boswell, B.A.2    Bachinger, H.P.3
  • 11
    • 0025968746 scopus 로고
    • Cyclosporin a slows collagen triple-helix formation in vivo: Indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase
    • B. Steinmann, P. Bruckner, and A. Superti-Furga Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase J. Biol. Chem. 266 1991 1299 1303
    • (1991) J. Biol. Chem. , vol.266 , pp. 1299-1303
    • Steinmann, B.1    Bruckner, P.2    Superti-Furga, A.3
  • 12
    • 0028072632 scopus 로고
    • Recombinant expression and properties of the Kunitz-type protease-inhibitor module from human type VI collagen alpha 3(VI) chain
    • U. Mayer, E. Poschl, R. Nischt, U. Specks, T.C. Pan, M.L. Chu, and R. Timpl Recombinant expression and properties of the Kunitz-type protease-inhibitor module from human type VI collagen alpha 3(VI) chain Eur. J. Biochem. 225 1994 573 580
    • (1994) Eur. J. Biochem. , vol.225 , pp. 573-580
    • Mayer, U.1    Poschl, E.2    Nischt, R.3    Specks, U.4    Pan, T.C.5    Chu, M.L.6    Timpl, R.7
  • 13
    • 0027378858 scopus 로고
    • The alpha 1 beta 1 integrin recognition site of the basement membrane collagen molecule [alpha 1(IV)]2 alpha 2(IV)
    • J.A. Eble, R. Golbik, K. Mann, and K. Kuhn The alpha 1 beta 1 integrin recognition site of the basement membrane collagen molecule [alpha 1(IV)]2 alpha 2(IV) EMBO J. 12 1993 4795 4802
    • (1993) EMBO J. , vol.12 , pp. 4795-4802
    • Eble, J.A.1    Golbik, R.2    Mann, K.3    Kuhn, K.4
  • 14
    • 0020355552 scopus 로고
    • Mouse procollagen IV. Characterization and supramolecular association
    • H.P. Bachinger, L.I. Fessler, and J.H. Fessler Mouse procollagen IV. Characterization and supramolecular association J. Biol. Chem. 257 1982 9796 9803
    • (1982) J. Biol. Chem. , vol.257 , pp. 9796-9803
    • Bachinger, H.P.1    Fessler, L.I.2    Fessler, J.H.3
  • 15
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • F.L. Graham, and A.J. van der Eb A new technique for the assay of infectivity of human adenovirus 5 DNA Virology 52 1973 456 467
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 16
    • 0024232659 scopus 로고
    • The complete primary structure of the alpha 2 chain of human type IV collagen and comparison with the alpha 1(IV) chain
    • S.L. Hostikka, and K. Tryggvason The complete primary structure of the alpha 2 chain of human type IV collagen and comparison with the alpha 1(IV) chain J. Biol. Chem. 263 1988 19488 19493
    • (1988) J. Biol. Chem. , vol.263 , pp. 19488-19493
    • Hostikka, S.L.1    Tryggvason, K.2
  • 17
    • 0027516218 scopus 로고
    • Mechanisms of collagen trimer formation. Construction and expression of a recombinant minigene in HeLa cells reveals a direct effect of prolyl hydroxylation on chain assembly of type XII collagen
    • M. Mazzorana, H. Gruffat, A. Sergeant, and R.M. van der Mechanisms of collagen trimer formation. Construction and expression of a recombinant minigene in HeLa cells reveals a direct effect of prolyl hydroxylation on chain assembly of type XII collagen J. Biol. Chem. 268 1993 3029 3032
    • (1993) J. Biol. Chem. , vol.268 , pp. 3029-3032
    • Mazzorana, M.1    Gruffat, H.2    Sergeant, A.3    Van Der, R.M.4
  • 18
    • 0037163051 scopus 로고    scopus 로고
    • Crystal structure of NC1 domains. Structural basis for type IV collagen assembly in basement membranes
    • M. Sundaramoorthy, M. Meiyappan, P. Todd, and B.G. Hudson Crystal structure of NC1 domains. Structural basis for type IV collagen assembly in basement membranes J. Biol. Chem. 277 2002 31142 31153
    • (2002) J. Biol. Chem. , vol.277 , pp. 31142-31153
    • Sundaramoorthy, M.1    Meiyappan, M.2    Todd, P.3    Hudson, B.G.4
  • 19
    • 0034730769 scopus 로고    scopus 로고
    • Type IV collagen of the glomerular basement membrane. Evidence that the chain specificity of network assembly is encoded by the noncollagenous NC1 domains
    • A. Boutaud, D.B. Borza, O. Bondar, S. Gunwar, K.O. Netzer, N. Singh, Y. Ninomiya, Y. Sado, M.E. Noelken, and B.G. Hudson Type IV collagen of the glomerular basement membrane. Evidence that the chain specificity of network assembly is encoded by the noncollagenous NC1 domains J. Biol. Chem. 275 2000 30716 30724
    • (2000) J. Biol. Chem. , vol.275 , pp. 30716-30724
    • Boutaud, A.1    Borza, D.B.2    Bondar, O.3    Gunwar, S.4    Netzer, K.O.5    Singh, N.6    Ninomiya, Y.7    Sado, Y.8    Noelken, M.E.9    Hudson, B.G.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.