Proteolytic dissection of the isolated platelet fibrinogen receptor, integrin GPIIb/IIIa. Localization of GPIIb and GPIIIa sequences putatively involved in the subunit interface and in intrasubunit and intrachain contacts.

Proteolytic dissection of the isolated platelet fibrinogen receptor, integrin GPIIb/IIIa. Localization of GPIIb and GPIIIa sequences putatively involved in the subunit interface and in intrasubunit and intrachain contacts.

Item
http://www.wikidata.org/entity/Q42792964
Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit associationIntegrin structure: new twists and turns in dynamic cell adhesion.Characterization of the cDNA and genomic DNA sequence encoding for the platelet integrin alpha IIB and beta III in a horse with Glanzmann thrombasthenia.Folding of the conserved domain but not of flanking regions in the integrin beta2 subunit requires association with the alpha subunitModeling the alpha IIb beta 3 integrin solution conformation.A new alternative transcript encodes a 60 kDa truncated form of integrin beta 3Glanzmann thrombasthenia. Cooperation between sequence variants in cis during splice site selection.Extracellular Ca2+ modulates leukocyte function-associated antigen-1 cell surface distribution on T lymphocytes and consequently affects cell adhesion.A novel LFA-1 activation epitope maps to the I domain.Human neutrophil elastase proteolytically activates the platelet integrin alphaIIbbeta3 through cleavage of the carboxyl terminus of the alphaIIb subunit heavy chain. Involvement in the potentiation of platelet aggregation.The structure of the beta-propeller domain and C-terminal region of the integrin alphaM subunit. Dependence on beta subunit association and prediction of domains.Proteolytic degradation of the RGD-binding and non-RGD-binding conformers of human platelet integrin glycoprotein IIb/IIIa: clues for identification of regions involved in the receptor's activationInteractions of integrin GPIIb/IIIa-derived peptides with fibrinogen investigated by NMR spectroscopy.Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation.A Secondary Structure Model of the Integrin a Subunit N-Terminal Domain Based on Analysis of Multiple Alignments
P2860

Proteolytic dissection of the isolated platelet fibrinogen receptor, integrin GPIIb/IIIa. Localization of GPIIb and GPIIIa sequences putatively involved in the subunit interface and in intrasubunit and intrachain contacts.

Item
http://www.wikidata.org/entity/Q42792964
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Proteolytic dissection of the ...... bunit and intrachain contacts.
@en
Proteolytic dissection of the ...... bunit and intrachain contacts.
@nl
type
label
Proteolytic dissection of the ...... bunit and intrachain contacts.
@en
Proteolytic dissection of the ...... bunit and intrachain contacts.
@nl
prefLabel
Proteolytic dissection of the ...... bunit and intrachain contacts.
@en
Proteolytic dissection of the ...... bunit and intrachain contacts.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P478
P50
P577
P5875
P698
P921
P932
P356
P1433
P1476
Proteolytic dissection of the ...... bunit and intrachain contacts.
@en
P2093
P2860
P304
P31
P356
P407
P478
P50
P577
P5875
P698
P921
P932