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Volumn 8, Issue 9, 2013, Pages

Transmembrane and Juxtamembrane Structure of αL Integrin in Bicelles

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAIIB INTEGRIN; ALPHAL INTEGRIN; CD18 ANTIGEN; GLYCOPROTEIN; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 84884197364     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0074281     Document Type: Article
Times cited : (17)

References (57)
  • 2
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: are changes in affinity and conformation underemphasized?
    • Carman CV, Springer TA, (2003) Integrin avidity regulation: are changes in affinity and conformation underemphasized? Curr Opin Cell Biol 15: 547-556.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 547-556
    • Carman, C.V.1    Springer, T.A.2
  • 3
    • 0036683057 scopus 로고    scopus 로고
    • Role of integrins in regulating epidermal adhesion, growth and differentiation
    • Watt FM, (2002) Role of integrins in regulating epidermal adhesion, growth and differentiation. EMBO J 21: 3919-3926.
    • (2002) EMBO J , vol.21 , pp. 3919-3926
    • Watt, F.M.1
  • 4
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M, Carman CV, Springer TA, (2003) Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301: 1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 5
    • 0033517796 scopus 로고    scopus 로고
    • Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on αIIb β3 integrin conformation and oligomerization
    • Hantgan RR, Paumi C, Rocco M, Weisel JW, (1999) Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on αIIb β3 integrin conformation and oligomerization. Biochemistry 38: 14461-14474.
    • (1999) Biochemistry , vol.38 , pp. 14461-14474
    • Hantgan, R.R.1    Paumi, C.2    Rocco, M.3    Weisel, J.W.4
  • 7
    • 0035805633 scopus 로고    scopus 로고
    • Association of the membrane proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state
    • Lu CF, Takagi J, Springer TA, (2001) Association of the membrane proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state. J Biol Chem 276: 14642-14648.
    • (2001) J Biol Chem , vol.276 , pp. 14642-14648
    • Lu, C.F.1    Takagi, J.2    Springer, T.A.3
  • 8
    • 0028285015 scopus 로고
    • Integrin cytoplasmic domains mediate inside-out signal transduction
    • O'Toole TE, Katagiri Y, Faull RJ, Peter K, Tamura R, et al. (1994) Integrin cytoplasmic domains mediate inside-out signal transduction. J Cell Biol 124: 1047-1059.
    • (1994) J Cell Biol , vol.124 , pp. 1047-1059
    • O'Toole, T.E.1    Katagiri, Y.2    Faull, R.J.3    Peter, K.4    Tamura, R.5
  • 9
    • 0031181648 scopus 로고    scopus 로고
    • The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1
    • Lu CF, Springer TA, (1997) The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1. J Immunol 159: 268-278.
    • (1997) J Immunol , vol.159 , pp. 268-278
    • Lu, C.F.1    Springer, T.A.2
  • 10
    • 16644396938 scopus 로고    scopus 로고
    • A specific interface between integrin transmembrane helices and affinity for ligand
    • Luo BH, Springer TA, Takagi J, (2004) A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol 2: 776-786.
    • (2004) PLoS Biol , vol.2 , pp. 776-786
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 11
  • 12
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie KR, Prestegard JH, Engelman DM, (1997) A transmembrane helix dimer: Structure and implications. Science 276: 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 13
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin aIIbb3 based on electron cryomicroscopy and x-ray crystallography
    • Adair BD, Yeager M, (2002) Three-dimensional model of the human platelet integrin aIIbb3 based on electron cryomicroscopy and x-ray crystallography. Proc Nat Acad Sci USA 99: 14059-14064.
    • (2002) Proc Nat Acad Sci USA , vol.99 , pp. 14059-14064
    • Adair, B.D.1    Yeager, M.2
  • 14
    • 14844323604 scopus 로고    scopus 로고
    • Transmembrane domain helix packing stabilizes integrin alphaIIbbeta3 in the low affinity state
    • Partridge AW, Liu S, Kim S, Bowie JU, Ginsberg MH, (2005) Transmembrane domain helix packing stabilizes integrin alphaIIbbeta3 in the low affinity state. J Biol Chem 280: 7294-7300.
    • (2005) J Biol Chem , vol.280 , pp. 7294-7300
    • Partridge, A.W.1    Liu, S.2    Kim, S.3    Bowie, J.U.4    Ginsberg, M.H.5
  • 15
    • 64749101260 scopus 로고    scopus 로고
    • The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3
    • Zhu J, Luo BH, Barth P, Schonbrun J, Baker D, et al. (2009) The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3. Mol Cell 34: 234-249.
    • (2009) Mol Cell , vol.34 , pp. 234-249
    • Zhu, J.1    Luo, B.H.2    Barth, P.3    Schonbrun, J.4    Baker, D.5
  • 16
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau TL, Kim C, Ginsberg MH, Ulmer TS, (2009) The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J 28: 1351-1361.
    • (2009) EMBO J , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 17
    • 47049087659 scopus 로고    scopus 로고
    • Structure of the integrin alphaIIb transmembrane segment
    • Lau TL, Dua V, Ulmer TS, (2008) Structure of the integrin alphaIIb transmembrane segment. J Biol Chem 283: 16162-16168.
    • (2008) J Biol Chem , vol.283 , pp. 16162-16168
    • Lau, T.L.1    Dua, V.2    Ulmer, T.S.3
  • 18
    • 84873152707 scopus 로고    scopus 로고
    • NMR Structure of Integrin alpha4 Cytosolic Tail and Its Interactions with Paxillin
    • Chua GL, Patra AT, Tan SM, Bhattacharjya S, (2013) NMR Structure of Integrin alpha4 Cytosolic Tail and Its Interactions with Paxillin. PLoS ONE 8: e55184.
    • (2013) PLoS ONE , vol.8
    • Chua, G.L.1    Patra, A.T.2    Tan, S.M.3    Bhattacharjya, S.4
  • 19
    • 84864857773 scopus 로고    scopus 로고
    • Structure and binding interface of the cytosolic tails of alphaXbeta2 integrin
    • Chua GL, Tang XY, Patra AT, Tan SM, Bhattacharjya S, (2012) Structure and binding interface of the cytosolic tails of alphaXbeta2 integrin. PLoS ONE 7: e41924.
    • (2012) PLoS ONE , vol.7
    • Chua, G.L.1    Tang, X.Y.2    Patra, A.T.3    Tan, S.M.4    Bhattacharjya, S.5
  • 20
    • 83755171358 scopus 로고    scopus 로고
    • Structures and interaction analyses of integrin alphaMbeta2 cytoplasmic tails
    • Chua GL, Tang XY, Amalraj M, Tan SM, Bhattacharjya S, (2011) Structures and interaction analyses of integrin alphaMbeta2 cytoplasmic tails. J Biol Chem 286: 43842-43854.
    • (2011) J Biol Chem , vol.286 , pp. 43842-43854
    • Chua, G.L.1    Tang, X.Y.2    Amalraj, M.3    Tan, S.M.4    Bhattacharjya, S.5
  • 21
    • 63649107402 scopus 로고    scopus 로고
    • NMR solution conformations and interactions of integrin alphaLbeta2 cytoplasmic tails
    • Bhunia A, Tang XY, Mohanram H, Tan SM, Bhattacharjya S, (2009) NMR solution conformations and interactions of integrin alphaLbeta2 cytoplasmic tails. J Biol Chem 284: 3873-3884.
    • (2009) J Biol Chem , vol.284 , pp. 3873-3884
    • Bhunia, A.1    Tang, X.Y.2    Mohanram, H.3    Tan, S.M.4    Bhattacharjya, S.5
  • 22
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face
    • Vinogradova O, Velyvis A, Velyviene A, Hu B, Haas TA, et al. (2002) A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face. Cell 110: 587-597.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.A.5
  • 23
    • 0034652205 scopus 로고    scopus 로고
    • A structural basis for integrin activation by the cytoplasmic tail of the alpha(IIb)-subunit
    • Vinogradova O, Haas T, Plow EF, Qin J, (2000) A structural basis for integrin activation by the cytoplasmic tail of the alpha(IIb)-subunit. Proc Nat Acad Sci USA 97: 1450-1455.
    • (2000) Proc Nat Acad Sci USA , vol.97 , pp. 1450-1455
    • Vinogradova, O.1    Haas, T.2    Plow, E.F.3    Qin, J.4
  • 24
    • 84876970464 scopus 로고    scopus 로고
    • Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles
    • doi: 10.1371/journal.pone.0062954
    • Lai C, Liu X, Tian C, Wu F, (2013) Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles. PLOS ONe 8: e62954 doi:10.1371/journal.pone.0062954.
    • (2013) PLOS ONe , vol.8
    • Lai, C.1    Liu, X.2    Tian, C.3    Wu, F.4
  • 25
    • 45149128907 scopus 로고    scopus 로고
    • Protein Phosphatase 2A Negatively Regulates Integrin αIIbβ3 Signaling
    • Gushiken FC, Patel V, Liu Y, Pradhan S, Bergeron AL, et al. (2008) Protein Phosphatase 2A Negatively Regulates Integrin αIIbβ3 Signaling. J Biol Chem 283: 12862-12869.
    • (2008) J Biol Chem , vol.283 , pp. 12862-12869
    • Gushiken, F.C.1    Patel, V.2    Liu, Y.3    Pradhan, S.4    Bergeron, A.L.5
  • 26
    • 0034638831 scopus 로고    scopus 로고
    • Nischarin, a Novel Protein That Interacts with the Integrin α5 Subunit and Inhibits Cell Migration
    • Alahari SK, Lee JW, Juliano RL, (2000) Nischarin, a Novel Protein That Interacts with the Integrin α5 Subunit and Inhibits Cell Migration. J Cell Biol 151: 1141-1154.
    • (2000) J Cell Biol , vol.151 , pp. 1141-1154
    • Alahari, S.K.1    Lee, J.W.2    Juliano, R.L.3
  • 27
    • 0942290434 scopus 로고    scopus 로고
    • A membrane proximal region of the integrin alpha5 subunit is important for its interaction with nischarin
    • Alahari SK, Nasrallah H, (2004) A membrane proximal region of the integrin alpha5 subunit is important for its interaction with nischarin. Biochem J 377: 449-457.
    • (2004) Biochem J , vol.377 , pp. 449-457
    • Alahari, S.K.1    Nasrallah, H.2
  • 28
    • 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, (1999) Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits. J Biol Chem 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
  • 29
    • 0031046185 scopus 로고    scopus 로고
    • Identification of a Novel Calcium-binding Protein That Interacts with the Integrin αIIb Cytoplasmic Domain
    • Naik UP, Patel PM, Parise LV, (1997) Identification of a Novel Calcium-binding Protein That Interacts with the Integrin αIIb Cytoplasmic Domain. J Biol Chem 272: 4651-4654.
    • (1997) J Biol Chem , vol.272 , pp. 4651-4654
    • Naik, U.P.1    Patel, P.M.2    Parise, L.V.3
  • 30
    • 0037127264 scopus 로고    scopus 로고
    • Calcium Integrin-binding Protein Activates Platelet Integrin αIIbβ3
    • Tsuboi S, (2002) Calcium Integrin-binding Protein Activates Platelet Integrin αIIbβ3. J Biol Chem 277: 1919-1923.
    • (2002) J Biol Chem , vol.277 , pp. 1919-1923
    • Tsuboi, S.1
  • 31
    • 0033546169 scopus 로고    scopus 로고
    • Divalent Cations Differentially Regulate Integrin αIIb Cytoplasmic Tail Binding to β3 and to Calcium- and Integrin-binding Protein
    • Vallar L, Melchior C, Plançon S, Drobecq H, Lippens G, et al. (1999) Divalent Cations Differentially Regulate Integrin αIIb Cytoplasmic Tail Binding to β3 and to Calcium- and Integrin-binding Protein. J Biol Chem 274: 17257-17266.
    • (1999) J Biol Chem , vol.274 , pp. 17257-17266
    • Vallar, L.1    Melchior, C.2    Plançon, S.3    Drobecq, H.4    Lippens, G.5
  • 32
  • 33
    • 78650018068 scopus 로고    scopus 로고
    • Mammary-derived growth inhibitor (MDGI) interacts with integrin [alpha]-subunits and suppresses integrin activity and invasion
    • Nevo J, Mai A, Tuomi S, Pellinen T, Pentikainen OT, et al. (2010) Mammary-derived growth inhibitor (MDGI) interacts with integrin [alpha]-subunits and suppresses integrin activity and invasion. Oncogene 29: 6452-6463.
    • (2010) Oncogene , vol.29 , pp. 6452-6463
    • Nevo, J.1    Mai, A.2    Tuomi, S.3    Pellinen, T.4    Pentikainen, O.T.5
  • 34
    • 33947330922 scopus 로고    scopus 로고
    • Integrin regulation of lymphocyte trafficking: lessons from structural and signaling studies
    • Kinashi T, (2007) Integrin regulation of lymphocyte trafficking: lessons from structural and signaling studies. Adv Immunol 93: 185-227.
    • (2007) Adv Immunol , vol.93 , pp. 185-227
    • Kinashi, T.1
  • 35
    • 22344438374 scopus 로고    scopus 로고
    • Importance of integrin LFA-1 deactivation for the generation of immune responses
    • Semmrich M, Smith A, Feterowski C, Beer S, Engelhardt B, et al. (2005) Importance of integrin LFA-1 deactivation for the generation of immune responses. J Exp Med 201: 1987-1998.
    • (2005) J Exp Med , vol.201 , pp. 1987-1998
    • Semmrich, M.1    Smith, A.2    Feterowski, C.3    Beer, S.4    Engelhardt, B.5
  • 36
    • 77951926371 scopus 로고    scopus 로고
    • A transmembrane polar interaction is involved in the functional regulation of integrin αLβ2
    • Vararattanavech A, Chng CP, Parthasarathy K, Tang XY, Torres J, et al. (2010) A transmembrane polar interaction is involved in the functional regulation of integrin αLβ2. J Mol Biol 398: 569-583.
    • (2010) J Mol Biol , vol.398 , pp. 569-583
    • Vararattanavech, A.1    Chng, C.P.2    Parthasarathy, K.3    Tang, X.Y.4    Torres, J.5
  • 37
    • 59149102202 scopus 로고    scopus 로고
    • Disruption of the integrin alphaLbeta2 transmembrane domain interface by beta2 Thr-686 mutation activates alphaLbeta2 and promotes micro-clustering of the alphaL subunits
    • Vararattanavech A, Lin X, Torres J, Tan SM, (2009) Disruption of the integrin alphaLbeta2 transmembrane domain interface by beta2 Thr-686 mutation activates alphaLbeta2 and promotes micro-clustering of the alphaL subunits. J Biol Chem 284: 3239-3249.
    • (2009) J Biol Chem , vol.284 , pp. 3239-3249
    • Vararattanavech, A.1    Lin, X.2    Torres, J.3    Tan, S.M.4
  • 38
    • 79958706179 scopus 로고    scopus 로고
    • Proteins Struct Funct Bioinf
    • Chng CP, Tan SM, (2011) Proteins Struct Funct Bioinf. 79: 2203-2213.
    • (2011) , vol.79 , pp. 2203-2213
    • Chng, C.P.1    Tan, S.M.2
  • 39
    • 65649135871 scopus 로고    scopus 로고
    • Practical protocols for production of very high yields of recombinant proteins using Escherichia coli
    • Sivashanmugam A, Murray V, Cui CX, Zhang YH, Wang JJ, et al. (2009) Practical protocols for production of very high yields of recombinant proteins using Escherichia coli. Protein Sci 18: 936-948.
    • (2009) Protein Sci , vol.18 , pp. 936-948
    • Sivashanmugam, A.1    Murray, V.2    Cui, C.X.3    Zhang, Y.H.4    Wang, J.J.5
  • 40
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier FW, (2005) Protein production by auto-induction in high-density shaking cultures. Prot Exp Purif 41: 207-234.
    • (2005) Prot Exp Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 41
    • 0034721465 scopus 로고    scopus 로고
    • Alignment of Biopolymers in Strained Gels: A New Way To Create Detectable Dipole-Dipole Couplings in High-Resolution Biomolecular NMR
    • Tycko R, Blanco FJ, Ishii Y, (2000) Alignment of Biopolymers in Strained Gels: A New Way To Create Detectable Dipole-Dipole Couplings in High-Resolution Biomolecular NMR. J Am Chem Soc 122: 9340-9341.
    • (2000) J Am Chem Soc , vol.122 , pp. 9340-9341
    • Tycko, R.1    Blanco, F.J.2    Ishii, Y.3
  • 42
    • 0042367594 scopus 로고    scopus 로고
    • Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy
    • Ulmer TS, Ramirez BE, Delaglio F, Bax A, (2003) Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. J Am Chem Soc 125: 9179-9191.
    • (2003) J Am Chem Soc , vol.125 , pp. 9179-9191
    • Ulmer, T.S.1    Ramirez, B.E.2    Delaglio, F.3    Bax, A.4
  • 43
    • 0034884233 scopus 로고    scopus 로고
    • A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
    • Dosset P, Hus JC, Marion D, Blackledge M, (2001) A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings. J Biomol NMR 20: 223-231.
    • (2001) J Biomol NMR , vol.20 , pp. 223-231
    • Dosset, P.1    Hus, J.C.2    Marion, D.3    Blackledge, M.4
  • 44
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delaglio F, Bax A, (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13: 289-302.
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 45
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P, Mumenthaler C, Wuthrich K, (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273: 283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 46
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Guntert P, Wuthrich K, (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319: 209-227.
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55, 29-32.
    • (1996) J Mol Graph , vol.14
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 48
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT, (2007) Version 1.2 of the Crystallography and NMR system. Nat Prot 2: 2728-2733.
    • (2007) Nat Prot , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 51
    • 84861879108 scopus 로고    scopus 로고
    • Construction of Covalent Membrane Protein Complexes and High-Throughput Selection of Membrane Mimics
    • Suk J-E, Situ AJ, Ulmer TS, (2012) Construction of Covalent Membrane Protein Complexes and High-Throughput Selection of Membrane Mimics. J Am Chem Soc 134: 9030-9033.
    • (2012) J Am Chem Soc , vol.134 , pp. 9030-9033
    • Suk, J.-E.1    Situ, A.J.2    Ulmer, T.S.3
  • 52
    • 0031112791 scopus 로고    scopus 로고
    • Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides
    • Vold RR, Prosser RS, Deese AJ, (1997) Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides. J Biomol NMR 9: 329-335.
    • (1997) J Biomol NMR , vol.9 , pp. 329-335
    • Vold, R.R.1    Prosser, R.S.2    Deese, A.J.3
  • 53
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin αIIbβ3: roles of the transmembrane and cytoplasmic domains
    • Li R, Babu CR, Lear JD, Wand AJ, Bennett JS, et al. (2001) Oligomerization of the integrin αIIbβ3: roles of the transmembrane and cytoplasmic domains. Proc Nat Acad Sci USA 98: 12462-12467.
    • (2001) Proc Nat Acad Sci USA , vol.98 , pp. 12462-12467
    • Li, R.1    Babu, C.R.2    Lear, J.D.3    Wand, A.J.4    Bennett, J.S.5
  • 55
    • 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, (1999) Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits. J Biol Chem 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


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