Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb.
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Summary
It could be established that each cysteine residue in GPIIb, beginning at alpha-Cys-56, is disulphide-bonded to its nearest neighbour in the amino acid sequence, which will most probably be conserved in all two-chain alpha-subunits of these receptors.
- Type
- article
- Published
- 1989-07-15
- Cited by
- 65
- References
- 18
- Access
- Open access
- OpenAlex
- https://openalex.org/W637617399
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25721100
Keywords
Glycoprotein, Chemistry, Glycosylation, Amino acid, Biochemistry
References
- Interchain and intrachain disulphide bonds in human platelet glycoprotein IIb. Localization of the epitopes for several monoclonal antibodies.
- New isolation procedure and further biochemical characterization of glycoproteins IIb and IIIa from human platelet plasma membrane.
- Advanced Methods in Protein Microsequence Analysis
- Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors.
- Carbohydrate structure of human fibrinogen. Use of 300-MHz 1H-NMR to characterize glycosidase-treated glycopeptides.
- cDNA clones for human platelet GPIIb corresponding to mRNA from megakaryocytes and HEL cells. Evidence for an extensive homology to other Arg-Gly-Asp adhesion receptors.
- The platelet membrane glycoprotein IIb-IIIa complex.
- Comparison of cDNA-derived protein sequences of the human fibronectin and vitronectin receptor alpha-subunits and platelet glycoprotein IIb.
- Platelet glycoproteins IIb and IIIa: evidence for a family of immunologically and structurally related glycoproteins in mammalian cells.
- Molecular cloning and chemical synthesis of a region of platelet glycoprotein IIb involved in adhesive function.
- Biosynthesis and processing of platelet GPIIb-IIIa in human megakaryocytes
- Platelet glycoprotein IIb. Chromosomal localization and tissue expression.
- Isolation and biochemical characterization of the alpha- and beta-subunits of glycoprotein IIb of human platelet plasma membrane.
- Immunochemical characterization of the platelet-specific alloantigen Leka: a comparative study with the PlA1 alloantigen.
- Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa.
- Protein Sequence Determination
Cited by
- Ligand Binding to GPIIb-IIIa: A Status Report
- Integrins: versatility, modulation, and signaling in cell adhesion.
- Hemocompatibility of heparin-coated surfaces and the role of selective plasma protein adsorption.
- Clinical And Molecular Insights into Glanzmann’s Thrombasthenia in China
- Hämokompatibilität von Oxygenatoren mit kovalenter Heparinbeschichtung in einem HLM-Modell
- Integrins in the immune system.
- Glanzmann's thrombasthenia associated with deletion-insertion and alternative splicing in the glycoprotein IIb gene.
- Macrophages and Related Cells
- Characterisation of the Helix pomatia agglutinin binding glycoproteins of colorectal cancer cell lines and tissue samples
- Modeling the αIIbβ3 integrin solution conformation
- Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glycoprotein IIb/IIIa. Influence of peptide length.
- Collagen binding induces changes in its platelet integrin receptor alpha2beta1.
- 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 association.
- Three-dimensional Model of Human Platelet Integrin αIIbβ3 in Solution Obtained by Small Angle Neutron Scattering*
- Platelet membrane actin may be partially embedded in lipid bilayer and disulfide linked.
- Agonist-specific Structural Rearrangements of Integrin αIIbβ3
- Molecular characterization of the human platelet integrin GPIIb/IIIa and its constituent glycoproteins
- Structure of the Integrin VLA‐4 and its Cell‐Cell and Cell‐Matrix Adhesion Functions
- A large-scale procedure for the isolation of integrin GPIIb/IIIa, the human platelet fibrinogen receptor.
- Integrin Structure and Function in Hemostasis and Thrombosis
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