Civil Rights
Movements, leaders, victories and the continuing fight for equality.
Explore the people, places, events, achievements, struggles and stories that shaped our journey.
Movements, leaders, victories and the continuing fight for equality.
Innovation, patents, science, technology and world-changing contributions.
Pioneers, champions, Negro Leagues, records, activism and excellence.
Meet the people whose lives, choices and achievements shaped the journey.
Black towns, communities, institutions and places where history happened.
Moments that changed communities, movements, institutions and the nation.
Wilmington, North Carolina once had a thriving Black middle class and an elected interracial government. In 1898 white supremacists used violence to overthrow that government, kill Black residents and drive many others from the city.
MORE →Reflects the personal views, recollections, and perspective of the author, Mike Davis.
This is a personal recollection on the Move fire on May 13, 1985
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| Identifiers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | GP9, CD42a, GPIX, Glycoprotein IX, glycoprotein IX platelet | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 173515; MGI: 1860137; GeneCards: GP9 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
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Glycoprotein IX (platelet) (GP9) also known as CD42a (Cluster of Differentiation 42a), is a human gene.[5]
Platelet glycoprotein IX (GP9) is a small membrane glycoprotein found on the surface of human platelets. It forms a 1-to-1 noncovalent complex with glycoprotein Ib (GP Ib), a platelet surface membrane glycoprotein complex that functions as a receptor for von Willebrand factor (VWF; MIM 193400) (known as the Glycoprotein Ib-IX-V Receptor Complex). The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with GP9 and platelet glycoprotein V (GP5; MIM 173511).[supplied by OMIM][5]
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Source: Wikipedia. Article content is retrieved live through the MediaWiki API.
Glycoprotein IX (platelet) (GP9) also known as CD42a (Cluster of Differentiation 42a), is a human gene. Platelet glycoprotein IX (GP9) is a small membrane glycoprotein found on the surface of human platelets. It forms a 1-to-1 noncovalent complex with glycoprotein Ib (GP Ib), a platelet surface membrane glycoprotein complex that functions as a receptor for von Willebrand factor (VWF; MIM 193400) (known as the Glycoprotein Ib-IX-V Receptor Complex). The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with GP9 and platelet glycoprotein V (GP5; MIM 173511).[supplied by OMIM]
The GPIb-IX-V complex is a profuse membrane receptor complex originating in megakaryocytes and exclusively functional on the surface of platelets. It primarily functions to mediate the first critical step in platelet adhesion, by facilitating binding to von Willebrand factor (VWF) on damaged sub-endothelium under conditions of high fluid shear stress. Although the primary ligand for the GPIb-V-IX receptor is VWF, it can also bind to a number of other ligands in the circulation such as thrombin, P-selectin, factor XI, factor XII, high molecular weight kininogen as well as bacteria. GPIb-IX-V offers a critical role in thrombosis, metastasis, and the life cycle of platelets, and is implicated in a number of thrombotic pathological processes such as stroke or myocardial infarction.
Glycoprotein Ib (GPIb), also known as CD42, is a component of the GPIb-V-IX complex on platelets. The GPIb-V-IX complex binds von Willebrand factor, allowing platelet adhesion and platelet plug formation at sites of vascular injury. Glycoprotein Ibα (GPIbα) is the major ligand-binding subunit of the GPIb-V-IX complex. GPIbα is heavily glycosylated. It is deficient in the Bernard–Soulier syndrome. A gain-of-function mutation causes platelet-type von Willebrand disease. Autoantibodies against Ib/IX can be produced in immune thrombocytopenic purpura. Components include GP1BA and GP1BB. It complexes with Glycoprotein IX.
Glycoprotein V (platelet) (GP5) also known as CD42d (Cluster of Differentiation 42d), is a human gene. Human platelet glycoprotein V (GP5) is a part of the Ib-V-IX system of surface glycoproteins that constitute the receptor for von Willebrand factor (VWF; MIM 193400) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX (GP9; MIM 173515) and GP5. Mutations in GP1BA, GP1BB, and GP9 have been shown to cause Bernard-Soulier syndrome (MIM 231200), a bleeding disorder.[supplied by OMIM]
Before the 1921 destruction of Tulsa’s Greenwood District, Black residents had created a remarkable center of business and community life. The district included stores, professional offices, entertainment venues and homes owned by Black citizens. Understanding Greenwood means learning what was built—not only what was burned.
MORE →Shirley Chisholm, elected in 1968.