메뉴 건너뛰기




Volumn 408, Issue 3, 2007, Pages 347-354

Determination of protein regions responsible for interactions of amelogenin with CD63 and LAMP1

Author keywords

Amelogenin; CD63; Enamel matrix; Lysosome associated membrane protein 1 (LAMP1); Protein protein interaction; Yeast two hybrid assay

Indexed keywords

BIOASSAY; CELLS; HYDROXYAPATITE; YEAST;

EID: 37549021878     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070881     Document Type: Article
Times cited : (39)

References (53)
  • 2
    • 0242441731 scopus 로고    scopus 로고
    • Amelin: An enamel-related protein, transcribed in the cells of epithelial root sheath
    • Fong, C. D., Slaby, I. and Hammarstrom, L. (1996) Amelin: an enamel-related protein, transcribed in the cells of epithelial root sheath. J. Bone Miner. Res. 11, 892-898
    • (1996) J. Bone Miner. Res , vol.11 , pp. 892-898
    • Fong, C.D.1    Slaby, I.2    Hammarstrom, L.3
  • 5
    • 0032185624 scopus 로고    scopus 로고
    • Dentin sialoprotein, dentin phosphoprotein, enamelysin and ameloblastic tooth-specific molecules that are distinctively expressed during murine dental differentiation
    • Begue-Kirn, C., Krebsbach, P. H., Bartlett, J. D. and Butler, W. T. (1998) Dentin sialoprotein, dentin phosphoprotein, enamelysin and ameloblastic tooth-specific molecules that are distinctively expressed during murine dental differentiation. Eur.J. Oral Sci. 106, 963-970
    • (1998) Eur.J. Oral Sci , vol.106 , pp. 963-970
    • Begue-Kirn, C.1    Krebsbach, P.H.2    Bartlett, J.D.3    Butler, W.T.4
  • 8
    • 0030473811 scopus 로고    scopus 로고
    • Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ
    • Bartlett, J. D., Simmer, J. P., Xue, J., Margolis, H. C. and Moreno, E. C. (1996) Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ. Gene 183, 123-128
    • (1996) Gene , vol.183 , pp. 123-128
    • Bartlett, J.D.1    Simmer, J.P.2    Xue, J.3    Margolis, H.C.4    Moreno, E.C.5
  • 10
    • 33748794760 scopus 로고    scopus 로고
    • Role of macromolecular assembly of enamel matrix proteins in enamel formation
    • Margolis, H. C., Beniash, E. and Fowler, C. E. (2006) Role of macromolecular assembly of enamel matrix proteins in enamel formation. J. Dent. Res. 85, 775-793
    • (2006) J. Dent. Res , vol.85 , pp. 775-793
    • Margolis, H.C.1    Beniash, E.2    Fowler, C.E.3
  • 13
    • 0037409387 scopus 로고    scopus 로고
    • Tetraspanin proteins as organisers of membrane microdomains and signalling complexes
    • Yunta, M. and Lazo, P. A. (2003) Tetraspanin proteins as organisers of membrane microdomains and signalling complexes. Cell. Signalling 15, 559-564
    • (2003) Cell. Signalling , vol.15 , pp. 559-564
    • Yunta, M.1    Lazo, P.A.2
  • 14
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: More than meets the eye
    • Berditchevski, F. (2001) Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 114, 4143-4151
    • (2001) J. Cell Sci , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 16
    • 31544444139 scopus 로고    scopus 로고
    • Characterization of a mouse amelogenin [A-4]/M59 cell surface receptor
    • Tompkins, K., George, A. and Veis, A. (2006) Characterization of a mouse amelogenin [A-4]/M59 cell surface receptor. Bone 38, 172-180
    • (2006) Bone , vol.38 , pp. 172-180
    • Tompkins, K.1    George, A.2    Veis, A.3
  • 17
    • 4444227321 scopus 로고    scopus 로고
    • Lysosome associated membrane protein 1 (Lamp1) traffics directly from the TGN to early endosomes
    • Cook, N. R., Row, P. E. and Davidson, H. W. (2004) Lysosome associated membrane protein 1 (Lamp1) traffics directly from the TGN to early endosomes. Traffic 5, 685-699
    • (2004) Traffic , vol.5 , pp. 685-699
    • Cook, N.R.1    Row, P.E.2    Davidson, H.W.3
  • 18
    • 0030578410 scopus 로고    scopus 로고
    • Lysosome-associated membrane proteins h-LAMP1 (CD107a) and h-LAMP2 (CD107b) are activation-dependent cell surface glycoproteins in human peripheral blood mononuclear cells which mediate cell adhesion to vascular endothelium
    • Kannan, K., Stewart, R. M., Bounds, W., Carlsson, S. R., Fukuda, M., Betzing, K. W. and Holcombe, R. F. (1996) Lysosome-associated membrane proteins h-LAMP1 (CD107a) and h-LAMP2 (CD107b) are activation-dependent cell surface glycoproteins in human peripheral blood mononuclear cells which mediate cell adhesion to vascular endothelium. Cell. Immunol. 171, 10-19
    • (1996) Cell. Immunol , vol.171 , pp. 10-19
    • Kannan, K.1    Stewart, R.M.2    Bounds, W.3    Carlsson, S.R.4    Fukuda, M.5    Betzing, K.W.6    Holcombe, R.F.7
  • 21
    • 0032223595 scopus 로고    scopus 로고
    • Protein-to-protein interactions: Criteria defining the assembly of the enamel organic matrix
    • Paine, M. L., Krebsbach, P. H., Chen, L. S., Paine, C. T., Yamada, Y., Deutsch, D. and Snead, M. L. (1998) Protein-to-protein interactions: criteria defining the assembly of the enamel organic matrix. J. Dent. Res. 77, 496-502
    • (1998) J. Dent. Res , vol.77 , pp. 496-502
    • Paine, M.L.1    Krebsbach, P.H.2    Chen, L.S.3    Paine, C.T.4    Yamada, Y.5    Deutsch, D.6    Snead, M.L.7
  • 22
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • Adamczak, R., Porollo, A. and Meller, J. (2005) Combining prediction of secondary structure and solvent accessibility in proteins. Proteins 59, 467-475
    • (2005) Proteins , vol.59 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 24
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi, Z., Csizmok, V., Tompa, P. and Simon, I. (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J. Mol. Biol. 347, 827-839
    • (2005) J. Mol. Biol , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 25
    • 30344451365 scopus 로고    scopus 로고
    • Assessment of disorder prediclions in CASP6
    • Jin, Y. M. and Dunbrack, Jr, R. L. (2005) Assessment of disorder prediclions in CASP6. Proteins 61, 167-175
    • (2005) Proteins , vol.61 , pp. 167-175
    • Jin, Y.M.1    Dunbrack Jr, R.L.2
  • 26
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley, L. A., MacCallum, R. M. and Sternberg, M. J. E. (2000) Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299, 499-520
    • (2000) J. Mol. Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 28
    • 0037243301 scopus 로고    scopus 로고
    • Amelogenin self-assembly and the role of the proline located within the carboxyl-teleopeptide
    • Paine, M. L., Wang, H. J. and Snead, M. L. (2003) Amelogenin self-assembly and the role of the proline located within the carboxyl-teleopeptide. Connect. Tissue Res. 44, 52-57
    • (2003) Connect. Tissue Res , vol.44 , pp. 52-57
    • Paine, M.L.1    Wang, H.J.2    Snead, M.L.3
  • 31
    • 0031034185 scopus 로고    scopus 로고
    • Protein interactions during assembly of the enamel organic extracellular matrix
    • Paine, M. L. and Snead, M. L. (1997) Protein interactions during assembly of the enamel organic extracellular matrix. J. Bone Miner. Res. 12, 221-227
    • (1997) J. Bone Miner. Res , vol.12 , pp. 221-227
    • Paine, M.L.1    Snead, M.L.2
  • 33
    • 0036755086 scopus 로고    scopus 로고
    • Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop
    • Kitadokoro, K., Ponassi, M., Galli, G., Petracca, R., Falugi, F., Grandi, G. and Bolognesi, M. (2002) Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop. Biol. Chem. 383, 1447-1452
    • (2002) Biol. Chem , vol.383 , pp. 1447-1452
    • Kitadokoro, K.1    Ponassi, M.2    Galli, G.3    Petracca, R.4    Falugi, F.5    Grandi, G.6    Bolognesi, M.7
  • 34
    • 0007994445 scopus 로고
    • An X-ray diffraction pattern from human enamel matrix
    • Pautard, F. G. (1961) An X-ray diffraction pattern from human enamel matrix. Arch. Oral Biol. 3, 217-220
    • (1961) Arch. Oral Biol , vol.3 , pp. 217-220
    • Pautard, F.G.1
  • 35
    • 0015013799 scopus 로고
    • A polarization microscopic and micro X-ray diffraction study on organic matrix of developing human enamel
    • Angmar-Mansson, B. (1971) A polarization microscopic and micro X-ray diffraction study on organic matrix of developing human enamel. Arch. Oral Biol. 16, 147-156
    • (1971) Arch. Oral Biol , vol.16 , pp. 147-156
    • Angmar-Mansson, B.1
  • 36
    • 0345240480 scopus 로고
    • Developing enamel matrix proteins: A conformation study of enamelins and amelogenins
    • Jodaikin, A., Weiner, S., Perltreves, D., Traub. W. and Termine, J. D. (1987) Developing enamel matrix proteins: a conformation study of enamelins and amelogenins. Int. J. Biol. Macromol. 9, 166-168
    • (1987) Int. J. Biol. Macromol , vol.9 , pp. 166-168
    • Jodaikin, A.1    Weiner, S.2    Perltreves, D.3    Traub, W.4    Termine, J.D.5
  • 37
    • 25144524137 scopus 로고    scopus 로고
    • The onset of amelogenin nanosphere aggregation studied by small-angle X-ray scattering and dynamic light scattering
    • Aichmayer, B., Margolis, H. C., Sigel, R., Yamakoshi, Y., Simmer, J. P. and Fratzl, P. (2005) The onset of amelogenin nanosphere aggregation studied by small-angle X-ray scattering and dynamic light scattering. J. Struct. Biol. 151, 239-249
    • (2005) J. Struct. Biol , vol.151 , pp. 239-249
    • Aichmayer, B.1    Margolis, H.C.2    Sigel, R.3    Yamakoshi, Y.4    Simmer, J.P.5    Fratzl, P.6
  • 38
    • 14644413519 scopus 로고    scopus 로고
    • Supramolecular assembly of amelogenin nanospheres into birefringent microribbons
    • Du, C., Falini, G., Fermani, S., Abbott, C. and Moradian-Oldak, J. (2005) Supramolecular assembly of amelogenin nanospheres into birefringent microribbons. Science 307, 1450-1454
    • (2005) Science , vol.307 , pp. 1450-1454
    • Du, C.1    Falini, G.2    Fermani, S.3    Abbott, C.4    Moradian-Oldak, J.5
  • 39
    • 4644347747 scopus 로고    scopus 로고
    • The COOH terminus of the amelogenin, LRAP, is oriented next to the hydroxyapatite surface
    • Shaw, W. J., Campbell, A. A., Paine, M. L. and Snead, M. L. (2004) The COOH terminus of the amelogenin, LRAP, is oriented next to the hydroxyapatite surface. J. Biol. Chem. 279, 40263-40266
    • (2004) J. Biol. Chem , vol.279 , pp. 40263-40266
    • Shaw, W.J.1    Campbell, A.A.2    Paine, M.L.3    Snead, M.L.4
  • 40
    • 0027403490 scopus 로고
    • Molecular conformation of porcine amelogenin in solution: 3 folding units at the N-terminal, central, and C-terminal regions
    • Goto, Y., Kogure, E., Takagi, T., Aimoto, S. and Aoba, T. (1993) Molecular conformation of porcine amelogenin in solution: 3 folding units at the N-terminal, central, and C-terminal regions. J. Biochem. (Tokyo) 113, 55-60
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 55-60
    • Goto, Y.1    Kogure, E.2    Takagi, T.3    Aimoto, S.4    Aoba, T.5
  • 41
    • 0023431973 scopus 로고
    • A mixed β-turn and β-sheet structure for bovine tooth enamel amelogenin: Raman-spectroscopic evidence
    • Zheng, S. D., Tu, A. T., Renugopalakrishnan, V., Strawich, E. and Glimcher, M. J. (1987) A mixed β-turn and β-sheet structure for bovine tooth enamel amelogenin: Raman-spectroscopic evidence. Biopolymers 26, 1809-1813
    • (1987) Biopolymers , vol.26 , pp. 1809-1813
    • Zheng, S.D.1    Tu, A.T.2    Renugopalakrishnan, V.3    Strawich, E.4    Glimcher, M.J.5
  • 42
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J. and Wright, P. E. (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197-208
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 43
    • 84985720076 scopus 로고
    • 1H magnetic double-resonance study of fetal enamel matrix proteins
    • 1H magnetic double-resonance study of fetal enamel matrix proteins. Biopolymers 19, 741-750
    • (1980) Biopolymers , vol.19 , pp. 741-750
    • Termine, J.D.1    Torchia, D.A.2
  • 44
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F. and Jones, D. T. (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337, 635-645
    • (2004) J. Mol. Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 45
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A. L. (2005) Natively unfolded proteins. Curr. Opin. Struct. Biol. 15, 35-41
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 46
    • 0028519190 scopus 로고
    • Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light-scattering
    • Moradian-Oldak, J., Simmer, J. P., Lau, E. C., Sarte, P. E., Slavkin, H. C. and Fincham, A. G. (1994) Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light-scattering. Biopolymers 34, 1339-1347
    • (1994) Biopolymers , vol.34 , pp. 1339-1347
    • Moradian-Oldak, J.1    Simmer, J.P.2    Lau, E.C.3    Sarte, P.E.4    Slavkin, H.C.5    Fincham, A.G.6
  • 47
    • 0000086238 scopus 로고
    • The appearance of developing rat incisor enamel using a freeze fracturing technigue
    • Robinson, C., Fuchs, P. and Weatherell, J. A. (1981) The appearance of developing rat incisor enamel using a freeze fracturing technigue. J. Cryst. Growth 53, 160-165
    • (1981) J. Cryst. Growth , vol.53 , pp. 160-165
    • Robinson, C.1    Fuchs, P.2    Weatherell, J.A.3
  • 48
    • 0037237913 scopus 로고    scopus 로고
    • Amelogenin protein exhibits a modular design: Implications for form and function
    • Snead, M. L. (2003) Amelogenin protein exhibits a modular design: implications for form and function. Connect. Tissue Res. 44, 47-51
    • (2003) Connect. Tissue Res , vol.44 , pp. 47-51
    • Snead, M.L.1
  • 50
    • 0035955657 scopus 로고    scopus 로고
    • Structure of the tetraspanin main extracellular domain: A partially conserved fold with a structurally variable domain insertion
    • Seigneuret, M., Delaguillaumie, A., Lagaudriere-Gesbert, C. and Conjeaud, H. (2001) Structure of the tetraspanin main extracellular domain: a partially conserved fold with a structurally variable domain insertion. J. Biol. Chem. 276, 40055-40064
    • (2001) J. Biol. Chem , vol.276 , pp. 40055-40064
    • Seigneuret, M.1    Delaguillaumie, A.2    Lagaudriere-Gesbert, C.3    Conjeaud, H.4
  • 51
    • 0035162539 scopus 로고    scopus 로고
    • KAI1, a prostate metastasis suppressor: Prediction of solvated structure and interactions with binding partners: integrins, cadherins, and cell-surface receptor proteins
    • Bienstock, R. J. and Barrett, J. C. (2001) KAI1, a prostate metastasis suppressor: prediction of solvated structure and interactions with binding partners: integrins, cadherins, and cell-surface receptor proteins. Mol. Carcinog. 32, 139-153
    • (2001) Mol. Carcinog , vol.32 , pp. 139-153
    • Bienstock, R.J.1    Barrett, J.C.2
  • 52
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immune-signalling complexes
    • Levy, S. and Shoham, T. (2005) The tetraspanin web modulates immune-signalling complexes. Nat. Rev. Immunol. 5, 136-148
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 136-148
    • Levy, S.1    Shoham, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.