| D008024 |
Ligands |
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) |
Ligand |
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| D008969 |
Molecular Sequence Data |
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. |
Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular |
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| D009154 |
Mutation |
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. |
Mutations |
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| D001792 |
Blood Platelets |
Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation. |
Platelets,Thrombocytes,Blood Platelet,Platelet,Platelet, Blood,Platelets, Blood,Thrombocyte |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
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| D000818 |
Animals |
Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. |
Animal,Metazoa,Animalia |
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| D012910 |
Snake Venoms |
Solutions or mixtures of toxic and nontoxic substances elaborated by snake (Ophidia) salivary glands (Duvernoy's gland) for the purpose of killing prey or disabling predators and delivered by grooved or hollow fangs. They usually contain enzymes, toxins, and other factors. |
Duvernoy's Gland Secretion,Duvernoy's Secretion,Snake Toxin,Snake Toxins,Snake Venom,Duvernoy Gland Secretion,Duvernoy Secretion,Duvernoys Gland Secretion,Duvernoys Secretion,Secretion, Duvernoy's,Secretion, Duvernoy's Gland,Toxin, Snake,Venom, Snake |
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| D019038 |
Platelet Glycoprotein GPIb-IX Complex |
Platelet membrane glycoprotein complex essential for normal platelet adhesion and clot formation at sites of vascular injury. It is composed of three polypeptides, GPIb alpha, GPIb beta, and GPIX. Glycoprotein Ib functions as a receptor for von Willebrand factor and for thrombin. Congenital deficiency of the GPIb-IX complex results in Bernard-Soulier syndrome. The platelet glycoprotein GPV associates with GPIb-IX and is also absent in Bernard-Soulier syndrome. |
Antigens, CD42a,Antigens, CD42b,Antigens, CD42c,Antigens, CD42d,CD42a Antigens,CD42b Antigens,CD42c Antigens,CD42d Antigens,Platelet Membrane Glycoprotein IX,Platelet Membrane Glycoprotein Ib,Platelet Membrane Glycoprotein V,CD42a Antigen,CD42b Antigen,CD42c Antigen,CD42d Antigen,Glycoprotein Ib,Glycoprotein Ib alpha,Glycoprotein Ib beta,Glycoprotein Ib-IX Complex,Platelet Glycoprotein IX,Antigen, CD42a,Antigen, CD42b,Antigen, CD42c,Antigen, CD42d,Glycoprotein Ib IX Complex,Platelet Glycoprotein GPIb IX Complex |
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