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Items: 1 to 20 of 105


Tests of the extension and deadbolt models of integrin activation.

Zhu J, Boylan B, Luo BH, Newman PJ, Springer TA.

J Biol Chem. 2007 Apr 20;282(16):11914-20.


Integrin αII b tail distal of GFFKR participates in inside-out αII b β3 activation.

Li A, Guo Q, Kim C, Hu W, Ye F.

J Thromb Haemost. 2014 Jul;12(7):1145-55. doi: 10.1111/jth.12610.


Cooperative role of the membrane-proximal and -distal residues of the integrin beta3 cytoplasmic domain in regulation of talin-mediated alpha IIb beta3 activation.

Hato T, Yamanouchi J, Tamura T, Yakushijin Y, Sakai I, Yasukawa M.

J Biol Chem. 2008 Feb 29;283(9):5662-8. doi: 10.1074/jbc.M707246200.


A naturally occurring extracellular alpha-beta clasp contributes to stabilization of beta3 integrins in a bent, resting conformation.

Vomund AN, Stuhlsatz-Krouper S, Dimitry J, Song Y, Frazier WA.

Biochemistry. 2008 Nov 4;47(44):11616-24. doi: 10.1021/bi8015108.


Identification of interacting hot spots in the beta3 integrin stalk using comprehensive interface design.

Donald JE, Zhu H, Litvinov RI, DeGrado WF, Bennett JS.

J Biol Chem. 2010 Dec 3;285(49):38658-65. doi: 10.1074/jbc.M110.170670.


Identification of critical residues for regulation of integrin activation in the beta6-alpha7 loop of the integrin beta3 I-like domain.

Hato T, Yamanouchi J, Yakushijin Y, Sakai I, Yasukawa M.

J Thromb Haemost. 2006 Oct;4(10):2278-80. No abstract available.


Membrane-proximal {alpha}/{beta} stalk interactions differentially regulate integrin activation.

Kamata T, Handa M, Sato Y, Ikeda Y, Aiso S.

J Biol Chem. 2005 Jul 1;280(26):24775-83.


Structural requirements for activation in alphaIIb beta3 integrin.

Kamata T, Handa M, Ito S, Sato Y, Ohtani T, Kawai Y, Ikeda Y, Aiso S.

J Biol Chem. 2010 Dec 3;285(49):38428-37. doi: 10.1074/jbc.M110.139667.


The talin rod IBS2 alpha-helix interacts with the beta3 integrin cytoplasmic tail membrane-proximal helix by establishing charge complementary salt bridges.

Rodius S, Chaloin O, Moes M, Schaffner-Reckinger E, Landrieu I, Lippens G, Lin M, Zhang J, Kieffer N.

J Biol Chem. 2008 Aug 29;283(35):24212-23. doi: 10.1074/jbc.M709704200.


Critical residues for ligand binding in blade 2 of the propeller domain of the integrin alphaIIb subunit.

Tamura T, Hato T, Yamanouchi J, Fujita S.

Thromb Haemost. 2004 Jan;91(1):111-8.


Locking the beta3 integrin I-like domain into high and low affinity conformations with disulfides.

Luo BH, Takagi J, Springer TA.

J Biol Chem. 2004 Mar 12;279(11):10215-21.


Structure of an integrin with an alphaI domain, complement receptor type 4.

Xie C, Zhu J, Chen X, Mi L, Nishida N, Springer TA.

EMBO J. 2010 Feb 3;29(3):666-79. doi: 10.1038/emboj.2009.367.


Disruption of the beta3 663-687 disulfide bridge confers constitutive activity to beta3 integrins.

Butta N, Arias-Salgado EG, González-Manchón C, Ferrer M, Larrucea S, Ayuso MS, Parrilla R.

Blood. 2003 Oct 1;102(7):2491-7.


Role of the Helix in Talin F3 Domain (F3 Helix) in Talin-Mediated Integrin Activation.

Li A, Guo Q, Wei A, Zhou Y, Hu W.

Cell Biochem Biophys. 2017 Mar;75(1):79-86. doi: 10.1007/s12013-017-0781-x.


The novel S527F mutation in the integrin beta3 chain induces a high affinity alphaIIbbeta3 receptor by hindering adoption of the bent conformation.

Vanhoorelbeke K, De Meyer SF, Pareyn I, Melchior C, Plançon S, Margue C, Pradier O, Fondu P, Kieffer N, Springer TA, Deckmyn H.

J Biol Chem. 2009 May 29;284(22):14914-20. doi: 10.1074/jbc.M809167200.


The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity.

Hughes PE, O'Toole TE, Ylänne J, Shattil SJ, Ginsberg MH.

J Biol Chem. 1995 May 26;270(21):12411-7.


Identification of critical residues for ligand binding in the integrin beta3 I-domain by site-directed mutagenesis.

Yamanouchi J, Hato T, Tamura T, Fujita S.

Thromb Haemost. 2002 Apr;87(4):756-62.


Kindlins, integrin activation and the regulation of talin recruitment to αIIbβ3.

Kahner BN, Kato H, Banno A, Ginsberg MH, Shattil SJ, Ye F.

PLoS One. 2012;7(3):e34056. doi: 10.1371/journal.pone.0034056.

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