| 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 |
|
| D011487 |
Protein Conformation |
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). |
Conformation, Protein,Conformations, Protein,Protein Conformations |
|
| D002460 |
Cell Line |
Established cell cultures that have the potential to propagate indefinitely. |
Cell Lines,Line, Cell,Lines, Cell |
|
| D002462 |
Cell Membrane |
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. |
Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes |
|
| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D006863 |
Hydrogen-Ion Concentration |
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH |
pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations |
|
| D001665 |
Binding Sites |
The parts of a macromolecule that directly participate in its specific combination with another molecule. |
Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining |
|
| D013499 |
Surface Properties |
Characteristics or attributes of the outer boundaries of objects, including molecules. |
Properties, Surface,Property, Surface,Surface Property |
|
| D017434 |
Protein Structure, Tertiary |
The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. |
Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures |
|
| D050600 |
SNARE Proteins |
A superfamily of small proteins which are involved in the MEMBRANE FUSION events, intracellular protein trafficking and secretory processes. They share a homologous SNARE motif. The SNARE proteins are divided into subfamilies: QA-SNARES; QB-SNARES; QC-SNARES; and R-SNARES. The formation of a SNARE complex (composed of one each of the four different types SNARE domains (Qa, Qb, Qc, and R)) mediates MEMBRANE FUSION. Following membrane fusion SNARE complexes are dissociated by the NSFs (N-ETHYLMALEIMIDE-SENSITIVE FACTORS), in conjunction with SOLUBLE NSF ATTACHMENT PROTEIN, i.e., SNAPs (no relation to SNAP 25.) |
SNAP Receptor,SNARE Protein,NSF Attachment Protein Receptor,Receptor, SNAP,SNAP Receptors,SNARE,SNAREs,Soluble N-ethylmaleimide-Sensitive-Factor Attachment Protein Receptor,Target Membrane SNARE Proteins,Target SNARE Proteins,Vesicle SNARE Proteins,Vesicular SNARE Proteins,t-SNARE,tSNAREs,v-SNARE,v-SNAREs,Protein, SNARE,SNARE Proteins, Target,SNARE Proteins, Vesicle,SNARE Proteins, Vesicular,Soluble N ethylmaleimide Sensitive Factor Attachment Protein Receptor,v SNAREs |
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