| 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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| D009498 |
Neurotoxins |
Toxic substances from microorganisms, plants or animals that interfere with the functions of the nervous system. Most venoms contain neurotoxic substances. Myotoxins are included in this concept. |
Alpha-Neurotoxin,Excitatory Neurotoxin,Excitotoxins,Myotoxin,Myotoxins,Neurotoxin,Alpha-Neurotoxins,Excitatory Neurotoxins,Excitotoxin,Alpha Neurotoxin,Alpha Neurotoxins,Neurotoxin, Excitatory,Neurotoxins, Excitatory |
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| D010446 |
Peptide Fragments |
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. |
Peptide Fragment,Fragment, Peptide,Fragments, Peptide |
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| D010450 |
Endopeptidases |
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. |
Endopeptidase,Peptide Peptidohydrolases |
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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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| D012604 |
Scorpion Venoms |
Venoms from animals of the order Scorpionida of the class Arachnida. They contain neuro- and hemotoxins, enzymes, and various other factors that may release acetylcholine and catecholamines from nerve endings. Of the several protein toxins that have been characterized, most are immunogenic. |
Scorpion Toxin,Scorpion Toxins,Scorpion Venom Peptide,Tityus serrulatus Venom,Scorpion Venom,alpha-Scorpion Toxin,beta-Scorpion Toxin,gamma-Scorpion Toxin,Peptide, Scorpion Venom,Toxin, Scorpion,Toxin, alpha-Scorpion,Toxin, beta-Scorpion,Venom Peptide, Scorpion,Venom, Scorpion,Venom, Tityus serrulatus,alpha Scorpion Toxin,beta Scorpion Toxin,gamma Scorpion Toxin |
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| D012689 |
Sequence Homology, Nucleic Acid |
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function. |
Base Sequence Homology,Homologous Sequences, Nucleic Acid,Homologs, Nucleic Acid Sequence,Homology, Base Sequence,Homology, Nucleic Acid Sequence,Nucleic Acid Sequence Homologs,Nucleic Acid Sequence Homology,Sequence Homology, Base,Base Sequence Homologies,Homologies, Base Sequence,Sequence Homologies, Base |
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| D013329 |
Structure-Activity Relationship |
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. |
Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships |
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| D014357 |
Trypsin |
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. |
Tripcellim,Trypure,beta-Trypsin,beta Trypsin |
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