| HOME | Home Observation for Measurement of the Environment |
|---|---|
| MESCH | Multi-Environment Scheme |
| TPE | therapeutic plasma exchange; totally protected environment; typhoid-parathyroid enteritis |
| WES | wall echo sign; work environment scale |
| KAP study | Knowledge, Attitude & Practice study |
| signal peptides | Additional polypeptide sequence of 25 to 30 residues at the amino-terminal or carboxy-terminal end of proteins. The signal sequence signals the cellular fate or destination of a newly synthesised protein directing it to its ultimate destination in the cell. These leaders are recognised by the signal recognition particle and bound by specific receptor sites on the outer surface of the endoplasmic reticulum. They are then transported into the cisterna of the endoplasmic reticulum and from there directed to their ultimate destination in the cell. In prokaryotes, the signal peptides attach to the plasma membrane. These signal sequences are ultimately removed by specific peptidases. (12 Dec 1998) |
|---|---|
| signal processing, computer-assisted | Computer-assisted processing of electric, ultrasonic, or electronic signals to interpret function and activity. (12 Dec 1998) |
| signal recognition particle | A complex between a 7S RNA and six proteins. SRP binds to the nascent polypeptide chain of eukaryotic proteins with a signal sequence and halts further translation until the ribosome becomes associated with the rough endoplasmic reticulum. One of the SRP proteins (srp54) binds GTP and in association with 7SRNA and srp19 has GTPase activity. (18 Nov 1997) |
| signal recognition particle receptor | Receptor for the signal recognition particle (SRP) found in the membrane of the endoplasmic reticulum. Also called docking protein. Heterodimeric, both protomers having GTP binding capacity, though dissimilar binding sites. Not until the complex of SRP, ribosome, message and nascent polypeptide chain binds to the SRP receptor is the block to further chain elongation released and concurrently the SRP is released, leaving the ribosome attached to the endoplasmic reticulum membrane. Cotranslational transport of the polypeptide delivers it into the lumen of the ER. (18 Nov 1997) |
| signal response coupling | The cascade of processes by which an extracellular signal (typically a hormone or neurotransmitter) interacts with a receptor at the cell surface, causing a change in the level of a second messenger for example calcium or cyclic AMP) and ultimately effects a change in the cells functioning (for example: triggering glucose uptake or initiating cell division). Can also be applied to sensory signal transduction, for example of light at photoreceptors. (18 Nov 1997) |
| signal sequence | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |
| signal-to-noise ratio | <microscopy> Also sometimes used as an abbreviation for serial number, can be somewhat confusing in the case of electronic equipment. (05 Aug 1998) |
| signal void | In magnetic resonance imaging, a region emitting no radiofrequency signal, either because there are no activated protons in the region (such as flowing blood) or because a different element predominates, particularly calcium. (05 Mar 2000) |
| nuclear localization signal | Short, predominantly basic amino acid sequences identified as nuclear import signals for some proteins. These sequences are believed to interact with specific receptors at nuclear pores. (12 Dec 1998) |