메뉴 건너뛰기




Volumn 102, Issue 4, 2003, Pages 1155-1159

New insights into the structural basis of integrin activation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA5 INTEGRIN; BETA3 INTEGRIN; GUANINE NUCLEOTIDE BINDING PROTEIN; INTEGRIN; MANGANESE;

EID: 0042739086     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-01-0334     Document Type: Review
Times cited : (161)

References (59)
  • 1
    • 0024293497 scopus 로고
    • Electron microscopy and structural model of human fibronectin receptor
    • Nermut MV, Green NM, Eason P, Yamada SS, Yamada KM. Electron microscopy and structural model of human fibronectin receptor. EMBO J. 1988;7:4093-4099.
    • (1988) EMBO J , vol.7 , pp. 4093-4099
    • Nermut, M.V.1    Green, N.M.2    Eason, P.3    Yamada, S.S.4    Yamada, K.M.5
  • 2
    • 0030611604 scopus 로고    scopus 로고
    • Integrin alphaIIb beta3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding
    • Erb EM, Tangemann K, Bohrmann B, Muller B, Engel J. Integrin alphaIIb beta3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding. Biochemistry. 1997;36:7395-7402.
    • (1997) Biochemistry , vol.36 , pp. 7395-7402
    • Erb, E.M.1    Tangemann, K.2    Bohrmann, B.3    Muller, B.4    Engel, J.5
  • 3
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes RO. Integrins: versatility, modulation and signaling in cell adhesion. Cell. 1992;69:11-26.
    • (1992) Cell , vol.69 , pp. 11-26
    • Hynes, R.O.1
  • 5
    • 0036696097 scopus 로고    scopus 로고
    • Integrin structure: New twists and turns in dynamic cell adhesion
    • Arnaout MA. Integrin structure: new twists and turns in dynamic cell adhesion. Immunol Rev. 2002;186:125-140.
    • (2002) Immunol Rev , vol.186 , pp. 125-140
    • Arnaout, M.A.1
  • 6
    • 0032567250 scopus 로고    scopus 로고
    • Two-stage activation for alpha5beta1 integrin binding to surface-adsorbed fibronectin
    • Garcia AJ, Takagi J, Boettiger D. Two-stage activation for alpha5beta1 integrin binding to surface-adsorbed fibronectin. J Biol Chem. 1998;273:34710-34715.
    • (1998) J Biol Chem , vol.273 , pp. 34710-34715
    • Garcia, A.J.1    Takagi, J.2    Boettiger, D.3
  • 7
    • 0029062047 scopus 로고
    • Energetics of leukocyte integrin activation
    • Cai TQ, Wright SD. Energetics of leukocyte integrin activation. J Biol Chem. 1995;270:14358-14365.
    • (1995) J Biol Chem , vol.270 , pp. 14358-14365
    • Cai, T.Q.1    Wright, S.D.2
  • 8
    • 0033517796 scopus 로고    scopus 로고
    • Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on alphaIIbbeta3 integrin conformation and oligomerization
    • Hantgan RR, Paumi C, Rocco M, Weisel JW. Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on alphaIIbbeta3 integrin conformation and oligomerization. Biochemistry. 1999;38:14461-14474.
    • (1999) Biochemistry , vol.38 , pp. 14461-14474
    • Hantgan, R.R.1    Paumi, C.2    Rocco, M.3    Weisel, J.W.4
  • 9
    • 0029617794 scopus 로고
    • Reversible inactivation of purified leukocyte integrin CR3 (CD11b/CD18, alpham beta2) by removal of divalent cations from a cryptic site
    • Cai TQ, Law SK, Zhao HR, Wright SD. Reversible inactivation of purified leukocyte integrin CR3 (CD11b/CD18, alpham beta2) by removal of divalent cations from a cryptic site. Cell Adhes Commun. 1995;3:399-406.
    • (1995) Cell Adhes Commun , vol.3 , pp. 399-406
    • Cai, T.Q.1    Law, S.K.2    Zhao, H.R.3    Wright, S.D.4
  • 10
    • 0032578007 scopus 로고    scopus 로고
    • Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin alphaIIb beta3
    • Hato T, Pampori N, Shattil SJ. Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin alphaIIb beta3. J Cell Biol. 1998;141:1685-1695.
    • (1998) J Cell Biol , vol.141 , pp. 1685-1695
    • Hato, T.1    Pampori, N.2    Shattil, S.J.3
  • 11
    • 0034507687 scopus 로고    scopus 로고
    • Chemokines trigger immediate beta2 integrin affinity and mobility changes: Differential regulation and roles in lymphocyte arrest under flow
    • Constantin G, Majeed M, Giagulli C, et al. Chemokines trigger immediate beta2 integrin affinity and mobility changes: differential regulation and roles in lymphocyte arrest under flow. Immunity. 2000;13:759-769.
    • (2000) Immunity , vol.13 , pp. 759-769
    • Constantin, G.1    Majeed, M.2    Giagulli, C.3
  • 13
    • 0030570726 scopus 로고    scopus 로고
    • Stimulation of platelet glycoprotein IIb-IIIa (alphaIIb beta3-integrin) functional activity by a monoclonal antibody to the N-terminal region of glycoprotein IIIa
    • Mazurov AV, Khaspekova SG, Byzova TV, et al. Stimulation of platelet glycoprotein IIb-IIIa (alphaIIb beta3-integrin) functional activity by a monoclonal antibody to the N-terminal region of glycoprotein IIIa. FEBS Lett. 1996;391:84-88.
    • (1996) FEBS Lett , vol.391 , pp. 84-88
    • Mazurov, A.V.1    Khaspekova, S.G.2    Byzova, T.V.3
  • 14
    • 0027979834 scopus 로고
    • A mechanism for divalent cation regulation of beta3-integrins
    • Smith JW, Piotrowicz RS, Mathis D. A mechanism for divalent cation regulation of beta3-integrins. J Biol Chem. 1994;269:960-967.
    • (1994) J Biol Chem , vol.269 , pp. 960-967
    • Smith, J.W.1    Piotrowicz, R.S.2    Mathis, D.3
  • 15
    • 0027525561 scopus 로고
    • Long range propagation of conformational changes in integrin alphaIIb beta3
    • Du X, Gu M, Weisel JW, et al. Long range propagation of conformational changes in integrin alphaIIb beta3. J Biol Chem. 1993;268:23087-23092.
    • (1993) J Biol Chem , vol.268 , pp. 23087-23092
    • Du, X.1    Gu, M.2    Weisel, J.W.3
  • 16
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alphaV beta3
    • Xiong JP, Stehle T, Diefenbach B, et al. Crystal structure of the extracellular segment of integrin alphaV beta3. Science. 2001;294:339-345.
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.P.1    Stehle, T.2    Diefenbach, B.3
  • 17
  • 18
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extra-cellular domains in outside-in and inside-out signaling
    • Takagi J, Petre BM, Walz T, Springer TA. Global conformational rearrangements in integrin extra-cellular domains in outside-in and inside-out signaling. Cell. 2002;110:599-511.
    • (2002) Cell , vol.110 , pp. 599-511
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 19
    • 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 MA. A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell. 1993;72:857-867.
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 20
    • 0028986196 scopus 로고
    • Crystal structure of the A-domain from the α-subunit of β2 integrin complement receptor type 3 (CR3, CD11b/CD18)
    • Lee J-O, Rieu P, Arnaout MA, Liddington R. Crystal Structure of the A-domain from the α-subunit of β2 integrin complement receptor type 3 (CR3, CD11b/CD18). Cell. 1995;80:631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 21
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): A pathway for activation?
    • Lee J-O, Anne-Bankston L, Arnaout MA, Liddington RC. Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure. 1995;3:1333-1340.
    • (1995) Structure , vol.3 , pp. 1333-1340
    • Lee, J.-O.1    Anne-Bankston, L.2    Arnaout, M.A.3    Liddington, R.C.4
  • 22
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • Beglova N, Blacklow SC, Takagi J, Springer TA. Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation. Nat Struct Biol. 2002;9:282-287.
    • (2002) Nat Struct Biol , vol.9 , pp. 282-287
    • Beglova, N.1    Blacklow, S.C.2    Takagi, J.3    Springer, T.A.4
  • 23
    • 0035041854 scopus 로고    scopus 로고
    • C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1
    • Takagi J, Erickson HP, Springer TA. C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1. Nat Struct Biol. 2001;8:412-416.
    • (2001) Nat Struct Biol , vol.8 , pp. 412-416
    • Takagi, J.1    Erickson, H.P.2    Springer, T.A.3
  • 24
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alphaV beta3 in complex with an Arg-Gly-Asp ligand
    • Xiong JP, Stehle T, Zhang R, et al. Crystal structure of the extracellular segment of integrin alphaV beta3 in complex with an Arg-Gly-Asp ligand. Science. 2002;296:151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3
  • 25
    • 0035965303 scopus 로고    scopus 로고
    • Evidence that ligand and metal ion binding to integrin alpha4 beta1 are regulated through a coupled equilibrium
    • Chen LL, Whitty A, Scott D, et al. Evidence that ligand and metal ion binding to integrin alpha4 beta1 are regulated through a coupled equilibrium. J Biol Chem. 2001;276:36520-36529.
    • (2001) J Biol Chem , vol.276 , pp. 36520-36529
    • Chen, L.L.1    Whitty, A.2    Scott, D.3
  • 26
    • 0029593456 scopus 로고
    • The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2
    • Wall MA, Coleman DE, Lee E, et al. The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. Cell. 1995;83:1047-1058.
    • (1995) Cell , vol.83 , pp. 1047-1058
    • Wall, M.A.1    Coleman, D.E.2    Lee, E.3
  • 27
    • 0034744186 scopus 로고    scopus 로고
    • Super-activation of integrin alphavbeta3 by low antagonist concentrations
    • Legler DF, Wiedle G, Ross FP, Imhof BA. Super-activation of integrin alphavbeta3 by low antagonist concentrations. J Cell Sci. 2001;114:1545-1553.
    • (2001) J Cell Sci , vol.114 , pp. 1545-1553
    • Legler, D.F.1    Wiedle, G.2    Ross, F.P.3    Imhof, B.A.4
  • 28
    • 0031854334 scopus 로고    scopus 로고
    • The 'ligand-induced conformational change' of alpha 5 beta 1 integrin. Relocation of alpha5 subunit to uncover the beta1 stalk region
    • Tsuchida J, Ueki S, Takada Y, Saito Y, Takagi J. The 'ligand-induced conformational change' of alpha 5 beta 1 integrin. Relocation of alpha5 subunit to uncover the beta1 stalk region. J Cell Sci. 1998;111(pt 12):f759-1766.
    • (1998) J Cell Sci , vol.111 , Issue.PART 12
    • Tsuchida, J.1    Ueki, S.2    Takada, Y.3    Saito, Y.4    Takagi, J.5
  • 29
    • 0029090806 scopus 로고
    • The activation state of the integrin alpha IIb beta 3 affects outside-in signals leading to cell spreading and focal adhesion kinase phosphorylation
    • Pelletier AJ, Kunicki T, Ruggeri ZM, Quaranta V. The activation state of the integrin alpha IIb beta 3 affects outside-in signals leading to cell spreading and focal adhesion kinase phosphorylation. J Biol Chem. 1995;270:18133-18140.
    • (1995) J Biol Chem , vol.270 , pp. 18133-18140
    • Pelletier, A.J.1    Kunicki, T.2    Ruggeri, Z.M.3    Quaranta, V.4
  • 30
    • 0026331367 scopus 로고
    • A highly conserved sequence of the Arg-Gly-Asp-binding domain of the integrin beta3 subunit is sensitive to stimulation
    • Andrieux A, Rabiet MJ, Chapel A, Concord E, Marguerie G. A highly conserved sequence of the Arg-Gly-Asp-binding domain of the integrin beta3 subunit is sensitive to stimulation. J Biol Chem. 1991;266:14202-14207.
    • (1991) J Biol Chem , vol.266 , pp. 14202-14207
    • Andrieux, A.1    Rabiet, M.J.2    Chapel, A.3    Concord, E.4    Marguerie, G.5
  • 31
    • 0028070770 scopus 로고
    • Activation of the fibrinogen binding site on platelets isolated from a patient with the Strasbourg I variant of Glanzmann's thrombasthenia
    • Kouns WC, Steiner B, Kunicki TJ, et al. Activation of the fibrinogen binding site on platelets isolated from a patient with the Strasbourg I variant of Glanzmann's thrombasthenia. Blood. 1994;84:1108-1115.
    • (1994) Blood , vol.84 , pp. 1108-1115
    • Kouns, W.C.1    Steiner, B.2    Kunicki, T.J.3
  • 32
    • 0028940694 scopus 로고
    • On the structure and function of platelet integrin alphaIIb beta3, the fibrinogen receptor
    • Calvete JJ. On the structure and function of platelet integrin alphaIIb beta3, the fibrinogen receptor. Proc Soc Exp Biol Med. 1995;208:346-360.
    • (1995) Proc Soc Exp Biol Med , vol.208 , pp. 346-360
    • Calvete, J.J.1
  • 33
    • 0035956887 scopus 로고    scopus 로고
    • Locking in alternate conformations of the integrin alphaL beta2 I domain with disulfide bonds reveals functional relationships among integrin domains
    • Lu C, Shimaoka M, Zang Q, Takagi J, Springer TA. Locking in alternate conformations of the integrin alphaL beta2 I domain with disulfide bonds reveals functional relationships among integrin domains. Proc Natl Acad Sci U S A. 2001;98:2393-2398.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2393-2398
    • Lu, C.1    Shimaoka, M.2    Zang, Q.3    Takagi, J.4    Springer, T.A.5
  • 34
    • 0037205483 scopus 로고    scopus 로고
    • Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain
    • Mould AP, Askari JA, Barton S, et al. Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain. J Biol Chem. 2002;277:19800-19805.
    • (2002) J Biol Chem , vol.277 , pp. 19800-19805
    • Mould, A.P.1    Askari, J.A.2    Barton, S.3
  • 35
    • 0034629281 scopus 로고    scopus 로고
    • Probing chemical and conformational differences in the resting and active conformers of platelet integrin alphaIIb beta3
    • Yan B, Hu DD, Knowles SK, Smith JW. Probing chemical and conformational differences in the resting and active conformers of platelet integrin alphaIIb beta3. J Biol Chem. 2000;275:7249-7260.
    • (2000) J Biol Chem , vol.275 , pp. 7249-7260
    • Yan, B.1    Hu, D.D.2    Knowles, S.K.3    Smith, J.W.4
  • 36
    • 0025781381 scopus 로고
    • Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex
    • Sims PJ, Ginsberg MH, Plow EF, Shattil SJ. Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex. J Biol Chem. 1991;266:7345-7352.
    • (1991) J Biol Chem , vol.266 , pp. 7345-7352
    • Sims, P.J.1    Ginsberg, M.H.2    Plow, E.F.3    Shattil, S.J.4
  • 37
    • 0029018097 scopus 로고
    • Involvement of the cysteine-rich domain of glycoprotein IIIa in the expression of the human platelet alloantigen, PIA 1: Evidence for heterogeneity in the humoral response
    • Valentin N, Visentin GP, Newman PJ. Involvement of the cysteine-rich domain of glycoprotein IIIa in the expression of the human platelet alloantigen, PIA 1: evidence for heterogeneity in the humoral response. Blood. 1995;85:3028-3033.
    • (1995) Blood , vol.85 , pp. 3028-3033
    • Valentin, N.1    Visentin, G.P.2    Newman, P.J.3
  • 38
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography
    • Adair BD, Yeager M. Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography. Proc Natl Acad Sci U S A. 2002;99:14059-14064.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14059-14064
    • Adair, B.D.1    Yeager, M.2
  • 39
    • 0037131270 scopus 로고    scopus 로고
    • Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation
    • Calzada MJ, Alvarez MV, Gonzalez-Rodriguez J. Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation. J Biol Chem. 2002;277:39899-39908.
    • (2002) J Biol Chem , vol.277 , pp. 39899-39908
    • Calzada, M.J.1    Alvarez, M.V.2    Gonzalez-Rodriguez, J.3
  • 40
    • 0033546144 scopus 로고    scopus 로고
    • Peptide ligands can bind to distinct sites in integrin alphaIIbbeta3 and elicit different functional responses
    • Cierniewski CS, Byzova T, Papierak M, et al. Peptide ligands can bind to distinct sites in integrin alphaIIbbeta3 and elicit different functional responses. J Biol Chem. 1999;274:16923-16932.
    • (1999) J Biol Chem , vol.274 , pp. 16923-16932
    • Cierniewski, C.S.1    Byzova, T.2    Papierak, M.3
  • 41
    • 0034625083 scopus 로고    scopus 로고
    • NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding
    • Huth JR, Olejniczak ET, Mendoza R, et al. NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding. Proc Natl Acad Sci U S A. 2000;97:5231-5236.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5231-5236
    • Huth, J.R.1    Olejniczak, E.T.2    Mendoza, R.3
  • 42
    • 0034624058 scopus 로고    scopus 로고
    • An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
    • Xiong JP, Li R, Essafi M, Stehle T, Arnaout MA. An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J Biol Chem. 2000;275:38762-38767.
    • (2000) J Biol Chem , vol.275 , pp. 38762-38767
    • Xiong, J.P.1    Li, R.2    Essafi, M.3    Stehle, T.4    Arnaout, M.A.5
  • 43
    • 0033543673 scopus 로고    scopus 로고
    • Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11 a I-domain
    • Kallen J, Welzenbach K, Ramage P, et al. Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11 a I-domain. J Mol Biol. 1999;292:1-9.
    • (1999) J Mol Biol , vol.292 , pp. 1-9
    • Kallen, J.1    Welzenbach, K.2    Ramage, P.3
  • 44
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin alphaIIb beta3 "inside-out" activation as regulated by its cytoplasmic face
    • Vinogradova O, Velyvis A, Velyviene A, et al. A structural mechanism of integrin alphaIIb beta3 "inside-out" activation as regulated by its cytoplasmic face. Cell. 2002;110:587-597.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3
  • 45
    • 0033601259 scopus 로고    scopus 로고
    • Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits
    • Armulik A, Nilsson I, von Heijne G, Johansson S. Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits. J Biol Chem. 1999;274:37030-37034.
    • (1999) J Biol Chem , vol.274 , pp. 37030-37034
    • Armulik, A.1    Nilsson, I.2    Von Heijne, G.3    Johansson, S.4
  • 46
    • 0036087390 scopus 로고    scopus 로고
    • Transmembrane signal transduction of the alpha (IIb)beta(3) integrin
    • Gottschalk KE, Adams PD, Brunger AT, Kessler H. Transmembrane signal transduction of the alpha (IIb)beta(3) integrin. Protein Sci. 2002;11:1800-1812.
    • (2002) Protein Sci , vol.11 , pp. 1800-1812
    • Gottschalk, K.E.1    Adams, P.D.2    Brunger, A.T.3    Kessler, H.4
  • 47
  • 48
    • 0029671071 scopus 로고    scopus 로고
    • Control of beta1 integrin function. Localization of stimulatory epitopes
    • Wilkins JA, Li A, Ni H, Stupack DG, Shen C. Control of beta1 integrin function. Localization of stimulatory epitopes. J Biol Chem. 1996;271:3046-3051.
    • (1996) J Biol Chem , vol.271 , pp. 3046-3051
    • Wilkins, J.A.1    Li, A.2    Ni, H.3    Stupack, D.G.4    Shen, C.5
  • 49
    • 15844363687 scopus 로고    scopus 로고
    • Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain
    • Luque A, Gomez M, Puzon W, Takada Y, Sanchez-Madrid F, Cabanas C. Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain. J Biol Chem. 1996;271:11067-11075.
    • (1996) J Biol Chem , vol.271 , pp. 11067-11075
    • Luque, A.1    Gomez, M.2    Puzon, W.3    Takada, Y.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 50
    • 0029786408 scopus 로고    scopus 로고
    • Critical residues for ligand binding in an I domain-like structure of the integrin b1 subunit
    • Puzon-McLaughlin W, Takada Y. Critical residues for ligand binding in an I domain-like structure of the integrin b1 subunit. J Biol Chem. 1996;271:20438-20443.
    • (1996) J Biol Chem , vol.271 , pp. 20438-20443
    • Puzon-McLaughlin, W.1    Takada, Y.2
  • 51
    • 0034647506 scopus 로고    scopus 로고
    • Structural and functional studies with antibodies to the integrin beta2 subunit. A model for the I-like domain
    • Huang C, Zang Q, Takagi J, Springer TA. Structural and functional studies with antibodies to the integrin beta2 subunit. A model for the I-like domain. J Biol Chem. 2000;275:21514-21524.
    • (2000) J Biol Chem , vol.275 , pp. 21514-21524
    • Huang, C.1    Zang, Q.2    Takagi, J.3    Springer, T.A.4
  • 52
    • 0033561096 scopus 로고    scopus 로고
    • A mutation in the extracellular cysteine-rich repeat region of the beta3 subunit activates integrins alphaIIb beta3 and alphaV beta3
    • Kashiwagi H, Tomiyama Y, Tadokoro S, et al. A mutation in the extracellular cysteine-rich repeat region of the beta3 subunit activates integrins alphaIIb beta3 and alphaV beta3. Blood. 1999;93:2559-2568.
    • (1999) Blood , vol.93 , pp. 2559-2568
    • Kashiwagi, H.1    Tomiyama, Y.2    Tadokoro, S.3
  • 53
    • 0032578632 scopus 로고    scopus 로고
    • Three novel integrin beta3 subunit missense mutations (H280P, C560F, and G579S) in thrombasthenia, including one (H280P) prevalent in Japanese patients
    • Ambo H, Kamata T, Handa M, et al. Three novel integrin beta3 subunit missense mutations (H280P, C560F, and G579S) in thrombasthenia, including one (H280P) prevalent in Japanese patients. Biochem Biophys Res Commun. 1998;251:763-768.
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 763-768
    • Ambo, H.1    Kamata, T.2    Handa, M.3
  • 54
    • 0035914422 scopus 로고    scopus 로고
    • Probing conformational changes in the I-like domain and the cysteine-rich repeat of human beta3 integrins following disulfide bond disruption by cysteine mutations: Identification of cysteine 598 involved in alphaIIbbeta3 activation
    • Chen P, Melchior C, Brons NH, Schlegel N, Caen J, Kieffer N. Probing conformational changes in the I-like domain and the cysteine-rich repeat of human beta3 integrins following disulfide bond disruption by cysteine mutations: identification of cysteine 598 involved in alphaIIbbeta3 activation. J Biol Chem. 2001;276:38628-38635.
    • (2001) J Biol Chem , vol.276 , pp. 38628-38635
    • Chen, P.1    Melchior, C.2    Brons, N.H.3    Schlegel, N.4    Caen, J.5    Kieffer, N.6
  • 55
    • 0034617222 scopus 로고    scopus 로고
    • Molecular basis of ligand recognition by integrin alpha5 beta1, II: Specificity of Arg-Gly-Asp binding is determined by Trp 157 of the alpha subunit
    • Humphries JD, Askari JA, Zhang XP, Takada Y, Humphries MJ, Mould AP. Molecular basis of ligand recognition by integrin alpha5 beta1, II: specificity of Arg-Gly-Asp binding is determined by Trp 157 of the alpha subunit. J Biol Chem. 2000;275:20337-20345.
    • (2000) J Biol Chem , vol.275 , pp. 20337-20345
    • Humphries, J.D.1    Askari, J.A.2    Zhang, X.P.3    Takada, Y.4    Humphries, M.J.5    Mould, A.P.6
  • 56
    • 0026035170 scopus 로고
    • Assignment of disulphide bonds in human platelet GPIIIa: A disulphide pattern for the b-subunits of the integrin family
    • Calvete JJ, Henschen A, Gonzalez-Rodriguez J. Assignment of disulphide bonds in human platelet GPIIIa: a disulphide pattern for the b-subunits of the integrin family. Biochem J. 1991;274:63-71.
    • (1991) Biochem J , vol.274 , pp. 63-71
    • Calvete, J.J.1    Henschen, A.2    Gonzalez-Rodriguez, J.3
  • 57
    • 0011878085 scopus 로고
    • Molecular cloning and chemical synthesis of a region of platelet glycoprotein IIb involved in adhesive function
    • Loftus JC, Plow EF, Frelinger AL 3rd, et al. Molecular cloning and chemical synthesis of a region of platelet glycoprotein IIb involved in adhesive function. Proc Natl Acad Sci U S A. 1987;84:7114-7118.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7114-7118
    • Loftus, J.C.1    Plow, E.F.2    Frelinger A.L. III3
  • 59
    • 0034479757 scopus 로고    scopus 로고
    • TOP: A new method for protein structure comparisons and similarity searches
    • Lu G. TOP: a new method for protein structure comparisons and similarity searches. J Appl. Cryst. 2000;33:176-183.
    • (2000) J Appl Cryst , vol.33 , pp. 176-183
    • Lu, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.