Примери коришћења Transmembrane на Енглеском и њихови преводи на Српски
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The B cell receptor(BCR)is a transmembrane protein on the surface of a B cell.
The transmembrane form can be cleaved from the membrane, generating a soluble protein fragment.
The third receptor has a single transmembrane domain and is encoded by the SORT1 gene.
It is a transmembrane receptor that is activated by a hormone called insulin-like growth factor 1(IGF-1) and by a related hormone called IGF-2.
It is named the cystic fibrosis transmembrane conductance regulator(CFTR).
The main ligand binding site is in the hydrophobic core between the loops andthe outer segments of transmembrane domains 3-7(TM3-TM7).
It is a cystic fibrosis transmembrane conductance regulator(CFTR) potentiator.
ABC transporters are minimally constituted of two conserved regions: a highly conserved ATP binding cassette(ABC) anda less conserved transmembrane domain(TMD).
They also have seven transmembrane domains, a characteristic unique to this subfamily.
Two of the receptors encoded by the NTSR1 andNTSR2 genes contain seven transmembrane helices and are G protein coupled.
Rotation and tilting of transmembrane α-helices may both contribute to these conformational changes.
They can be classified according to their relationship with the bilayer: Integral polytopic proteins are transmembrane proteins that span across the membrane more than once.
When only the transmembrane regions of the receptors are considered, amino acid similarity between the two receptor subtypes is approximately 68%.
Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains.
The insulin receptor(IR)is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of tyrosine kinase receptors.
They are characterized byan extracellular N terminus, 7 transmembrane regions, and an intracellular C terminus.
The gene product is a glycosylated transmembrane protein that functions in both the peripheral and central nervous system to modulate the release of various neurotransmitters.
GTPases play an important role in: Signal transduction at the intracellular domain of transmembrane receptors, including recognition of taste, smell and light.
In most exporters,the N-terminal transmembrane domain and the C-terminal ABC domains are fused as a single polypeptide chain, arranged as TMD-NBD-TMD-NBD.
The common feature of all ABC transporters is that they consist of two distinct domains, the transmembrane domain(TMD) and the nucleotide-binding domain(NBD).
Although BACE cleaves the extracellular domains of several transmembrane proteins, its physiological function remains unknown. citation needed Secretase at the US National Library of Medicine Medical Subject Headings(MeSH).
This enzyme catalyses the following chemical reaction Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains.
The neurotensin receptors are transmembrane receptors that bind the neurotransmitter neurotensin.
The FZD1 protein contains a signal peptide,a cysteine-rich domain in the N-terminal extracellular region, 7 transmembrane domains, and a C-terminal PDZ domain-binding motif.
Like other transmembrane receptors, acetylcholine receptors are classified according to their"pharmacology", or according to their relative affinities and sensitivities to different molecules.
ABC transporters often consist of multiple subunits,one or two of which are transmembrane proteins and one or two of which are membrane-associated ATPases.
The transmembrane subunit of the vitamin B12 importer, BtuCD,contains 10 TM helices and the functional unit consists of two copies each of the nucleotide binding domain(NBD) and transmembrane domain(TMD).
It is composed of281 amino acids and has characteristics of a type II transmembrane protein(i.e. no leader sequence and an internal transmembrane domain).
Receptors for most peptide as well as many eicosanoid hormones are embedded in the plasma membrane at the surface of the cell and the majority of thesereceptors belong to the G protein-coupled receptor(GPCR) class of seven alpha helix transmembrane proteins.
HMG-CoA reductase is anchored in the membrane of the endoplasmic reticulum, andwas long regarded as having seven transmembrane domains, with the active site located in a long carboxyl terminal domain in the cytosol.