메뉴 건너뛰기




Volumn 60, Issue 2, 1999, Pages 179-187

Cloning, sequence analysis, and chromosomal localization of the novel human integrin α11 subunit (ITGA11)

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN; MESSENGER RNA;

EID: 0033200036     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1999.5909     Document Type: Article
Times cited : (26)

References (51)
  • 3
    • 0024321304 scopus 로고
    • Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb
    • Calvete J. J., Henschen A., Gonzalez-Rodriguez J. Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb. Biochem. J. 261:1989;561-568.
    • (1989) Biochem. J. , vol.261 , pp. 561-568
    • Calvete, J.J.1    Henschen, A.2    Gonzalez-Rodriguez, J.3
  • 4
    • 0032493643 scopus 로고    scopus 로고
    • Isolation, cloning and sequence analysis of the integrin subunit α10, a β1-associated collagen binding integrin expressed on chondrocytes
    • Camper L., Hellman U., Lundgren-Åkerlund E. Isolation, cloning and sequence analysis of the integrin subunit α10, a β1-associated collagen binding integrin expressed on chondrocytes. J. Biol. Chem. 273:1998;20383-20389.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20383-20389
    • Camper, L.1    Hellman, U.2    Lundgren-Åkerlund, E.3
  • 5
    • 0030610917 scopus 로고    scopus 로고
    • Integrin α2β1 is a receptor for the cartilage protein chondroadherin
    • Camper L., Heinegard D., Lundgren-Åkerlund E. Integrin α2β1 is a receptor for the cartilage protein chondroadherin. J. Cell Biol. 138:1997;1159-1167.
    • (1997) J. Cell Biol. , vol.138 , pp. 1159-1167
    • Camper, L.1    Heinegard, D.2    Lundgren-Åkerlund, E.3
  • 7
    • 0023661323 scopus 로고
    • CDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p150,95
    • Corbi A. L., Miller L. J., O'Connor K., Larson R. S., Springer T. A. cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p150,95. EMBO J. 6:1987;4023-4028.
    • (1987) EMBO J. , vol.6 , pp. 4023-4028
    • Corbi, A.L.1    Miller, L.J.2    O'Connor, K.3    Larson, R.S.4    Springer, T.A.5
  • 8
    • 0029161166 scopus 로고
    • An alternatively spliced exon in the extracellular domain of the human α6 integrin subunit - Functional analysis of the α6 integrin variants
    • Delwel G. O., Kuikman I., Sonnenberg A. An alternatively spliced exon in the extracellular domain of the human α6 integrin subunit - Functional analysis of the α6 integrin variants. Cell Adhes. Commun. 3:1995;143-146.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 143-146
    • Delwel, G.O.1    Kuikman, I.2    Sonnenberg, A.3
  • 9
    • 0030690467 scopus 로고    scopus 로고
    • The two phenylalanines in the GFFKR motif of the integrin α6A subunit are essential for heterodimerization
    • De Melker A. A., Kramer D., Kuikman L., Sonnenberg A. The two phenylalanines in the GFFKR motif of the integrin α6A subunit are essential for heterodimerization. Biochem. J. 328:1997;529-537.
    • (1997) Biochem. J. , vol.328 , pp. 529-537
    • De Melker, A.A.1    Kramer, D.2    Kuikman, L.3    Sonnenberg, A.4
  • 10
    • 0031866394 scopus 로고    scopus 로고
    • Ligand recognition by the I domain-containing integrins
    • Dickeson S. K., Santoro S. A. Ligand recognition by the I domain-containing integrins. Cell. Mol. Life Sci. 54:1998;556-566.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 556-566
    • Dickeson, S.K.1    Santoro, S.A.2
  • 13
    • 0021028111 scopus 로고
    • Calcium cation regulation of glycoprotein IIb-IIIa complex formation in platelet plasma membranes
    • Fujimura K., Phillips D. R. Calcium cation regulation of glycoprotein IIb-IIIa complex formation in platelet plasma membranes. J. Biol. Chem. 258:1983;10247-10252.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10247-10252
    • Fujimura, K.1    Phillips, D.R.2
  • 14
    • 0029974250 scopus 로고    scopus 로고
    • Isolation of genes differentially expressed in human primary myoblasts and embryonal rhabdomyosarcoma
    • Genini M., Schwalbe P., Scholl F. A., Schafer B. W. Isolation of genes differentially expressed in human primary myoblasts and embryonal rhabdomyosarcoma. Int. J. Cancer. 66:1996;571-577.
    • (1996) Int. J. Cancer , vol.66 , pp. 571-577
    • Genini, M.1    Schwalbe, P.2    Scholl, F.A.3    Schafer, B.W.4
  • 16
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: Structures, functions, and their role on leukocytes
    • Hemler M. E. VLA proteins in the integrin family: Structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 8:1990;365-400.
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 17
    • 0025195762 scopus 로고
    • Structure of the integrin VLA-4 and its cell-cell and cell-matrix adhesion functions
    • Hemler M. E., Elices M. J., Parker C., Takada Y. Structure of the integrin VLA-4 and its cell-cell and cell-matrix adhesion functions. Immunol. Rev. 114:1990;45-65.
    • (1990) Immunol. Rev. , vol.114 , pp. 45-65
    • Hemler, M.E.1    Elices, M.J.2    Parker, C.3    Takada, Y.4
  • 18
    • 0028793281 scopus 로고
    • Chondrocyte and chondrosarcoma cell integrins with affinity for collagen type II and their response to mechanical stress
    • Holmvall K., Camper L., Johansson S., Rubin K., Kimura J. H., Lundgren-Åkerlund E. Chondrocyte and chondrosarcoma cell integrins with affinity for collagen type II and their response to mechanical stress. Exp. Cell Res. 221:1995;496-503.
    • (1995) Exp. Cell Res. , vol.221 , pp. 496-503
    • Holmvall, K.1    Camper, L.2    Johansson, S.3    Rubin, K.4    Kimura, J.H.5    Lundgren-Åkerlund, E.6
  • 19
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R. O. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 20
    • 0028075817 scopus 로고
    • Direct binding of collagen to the I domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner
    • Kamata T., Takada Y. Direct binding of collagen to the I domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner. J. Biol. Chem. 269:1994;26006-26010.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26006-26010
    • Kamata, T.1    Takada, Y.2
  • 23
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee J. O., Rieu P., Arnaout M. A., Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell. 80:1995;631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 24
    • 0032481294 scopus 로고    scopus 로고
    • A novel extracellular domain variant of the human integrin α7 subunit generated by alternative intron splicing
    • Leung E., Lim S. P., Berg R., Yang Y., Ni J., Wang S. X., Krissansen G. W. A novel extracellular domain variant of the human integrin α7 subunit generated by alternative intron splicing. Biochem. Biophys. Res. Commun. 243:1998;317-325.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 317-325
    • Leung, E.1    Lim, S.P.2    Berg, R.3    Yang, Y.4    Ni, J.5    Wang, S.X.6    Krissansen, G.W.7
  • 25
    • 0031181648 scopus 로고    scopus 로고
    • The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1
    • Lu C. F., Springer T. A. The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1. J. Immunol. 159:1997;268-278.
    • (1997) J. Immunol. , vol.159 , pp. 268-278
    • Lu, C.F.1    Springer, T.A.2
  • 27
    • 0030981877 scopus 로고    scopus 로고
    • Identification and characterization of neogenin, a DCC-related gene
    • Meyerhardt J. A., Look A. T., Bigner S. H., Fearon E. R. Identification and characterization of neogenin, a DCC-related gene. Oncogene. 14:1997;1129-1136.
    • (1997) Oncogene , vol.14 , pp. 1129-1136
    • Meyerhardt, J.A.1    Look, A.T.2    Bigner, S.H.3    Fearon, E.R.4
  • 28
    • 0027483226 scopus 로고
    • A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • Michishita M., Videm V., Arnaout M. A. A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell. 72:1993;857-867.
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 30
    • 0027268240 scopus 로고
    • Biochemical characterization of human osteoclast integrins. Osteoclasts express αvβ3, α2β1, and αvβ1 integrins
    • Nesbitt S., Nesbit A., Helfrich M., Horton M. Biochemical characterization of human osteoclast integrins. Osteoclasts express αvβ3, α2β1, and αvβ1 integrins. J. Biol. Chem. 268:1993;16737-16745.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16737-16745
    • Nesbitt, S.1    Nesbit, A.2    Helfrich, M.3    Horton, M.4
  • 31
    • 0030890648 scopus 로고    scopus 로고
    • Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins
    • Ni J., Abrahamson M., Zhang M., Fernandez M., Grubb A., Su J., Yu G.-L., Li Y.-L. Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins. J. Biol. Chem. 272:1997;10853-10858.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10853-10858
    • Ni, J.1    Abrahamson, M.2    Zhang, M.3    Fernandez, M.4    Grubb, A.5    Su, J.6    Yu, G.-L.7    Li, Y.-L.8
  • 32
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 34
    • 0014206483 scopus 로고
    • Two established in vitro cell lines from human mesenchymal tumours
    • Ponten J., Saksela E. Two established in vitro cell lines from human mesenchymal tumours. Int. J. Cancer. 2:1967;434-447.
    • (1967) Int. J. Cancer , vol.2 , pp. 434-447
    • Ponten, J.1    Saksela, E.2
  • 35
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αlβ2) integrin
    • Qu A., Leahy D. J. Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin. Proc. Natl. Acad. Sci. USA. 92:1995;10277-10281.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 36
    • 0028180681 scopus 로고
    • I domain of β2 integrin lymphocyte function-associated antigen-1 contains a binding site for ligand intercellular adhesion molecule-1
    • Randi A. M., Hogg N. I domain of β2 integrin lymphocyte function-associated antigen-1 contains a binding site for ligand intercellular adhesion molecule-1. J. Biol. Chem. 269:1994;12395-12398.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12395-12398
    • Randi, A.M.1    Hogg, N.2
  • 38
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E., Pierschbacher M. D. New perspectives in cell adhesion: RGD and integrins. Science. 238:1987;491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 39
    • 0027679403 scopus 로고
    • Integrin cytoplasmic domains: Mediators of cytoskeletal linkages and extra- And intracellular initiated transmembrane signaling
    • Sastry S. K., Horwitz A. F. Integrin cytoplasmic domains: Mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signaling. Curr. Opin. Cell Biol. 5:1993;819-831.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 819-831
    • Sastry, S.K.1    Horwitz, A.F.2
  • 41
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain
    • Springer T. A. Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain. Proc. Natl. Acad. Sci. USA. 94:1997;65-72.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 42
    • 0031566174 scopus 로고    scopus 로고
    • Fine mapping of five human skeletal muscle genes: Alpha-tropomyosin, beta-tropomyosin, troponin-I slow-twitch, troponin-I fast-twitch, and troponin-C fast
    • Tiso N., Rampoldi L., Pallavicini A., Zimbello R., Pandolfo Valle G., Lanfranchi G., Danieli G. A. Fine mapping of five human skeletal muscle genes: Alpha-tropomyosin, beta-tropomyosin, troponin-I slow-twitch, troponin-I fast-twitch, and troponin-C fast. Biochem. Biophys. Res. Commun. 230:1997;347-350.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 347-350
    • Tiso, N.1    Rampoldi, L.2    Pallavicini, A.3    Zimbello, R.4    Pandolfo, V.G.5    Lanfranchi, G.6    Danieli, G.A.7
  • 43
    • 0030320774 scopus 로고    scopus 로고
    • Ligand binding and affinity modulation of integrins
    • Tozer E. C., Hughes P. E., Loftus J. C. Ligand binding and affinity modulation of integrins. Biochem. Cell Biol. 74:1996;785-798.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 785-798
    • Tozer, E.C.1    Hughes, P.E.2    Loftus, J.C.3
  • 44
    • 0028054340 scopus 로고
    • A secondary structure model of the integrin alpha subunit N-terminal domain based on analysis of multiple alignments
    • Tuckwell D. S., Humphries M. J., Brass A. A secondary structure model of the integrin alpha subunit N-terminal domain based on analysis of multiple alignments. Cell Adhes. Comm. 2:1994;385-402.
    • (1994) Cell Adhes. Comm. , vol.2 , pp. 385-402
    • Tuckwell, D.S.1    Humphries, M.J.2    Brass, A.3
  • 45
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133:1983;17-21.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 46
    • 0030200219 scopus 로고    scopus 로고
    • The biochemistry of polyadenylation
    • Wahle E., Keller W. The biochemistry of polyadenylation. Trends Biochem. Sci. 21:1996;247-250.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 247-250
    • Wahle, E.1    Keller, W.2
  • 48
    • 0032078685 scopus 로고    scopus 로고
    • Oral squamous cell carcinomas are characterized by a rather uniform pattern of genomic imbalances detected by comparative genomic hybridisation
    • Wolff E., Girod S., Liehr T., Vorderwulbecke U., Ries J., Steininger H., Gebhart E. Oral squamous cell carcinomas are characterized by a rather uniform pattern of genomic imbalances detected by comparative genomic hybridisation. Oral Oncol. 34:1998;186-190.
    • (1998) Oral Oncol. , vol.34 , pp. 186-190
    • Wolff, E.1    Girod, S.2    Liehr, T.3    Vorderwulbecke, U.4    Ries, J.5    Steininger, H.6    Gebhart, E.7
  • 49
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada K. M., Miyamoto S. Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7:1995;681-689.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2
  • 50
    • 0031801882 scopus 로고    scopus 로고
    • Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia
    • Yavari R., Adida C., Bray-Ward P., Brines M., Xu T. Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia. Hum. Mol. Genet. 7:1998;1161-1167.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1161-1167
    • Yavari, R.1    Adida, C.2    Bray-Ward, P.3    Brines, M.4    Xu, T.5
  • 51
    • 0027454265 scopus 로고
    • Alternative extracellular and cytoplasmic domains of the integrin α7 subunit are differentially expressed during development
    • Ziober B. L., Vu M. P., Waleh N., Crawford J., Lin C. S., Kramer R. H. Alternative extracellular and cytoplasmic domains of the integrin α7 subunit are differentially expressed during development. J. Biol. Chem. 268:1993;26773-26783.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26773-26783
    • Ziober, B.L.1    Vu, M.P.2    Waleh, N.3    Crawford, J.4    Lin, C.S.5    Kramer, R.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.