Sentence examples for binding stress from inspiring English sources

Colligin 2 protein (also known as collagen binding stress protein; HSP 47) is localized in the endoplasmic reticulum and specifically binds to collagen type I, collagen type IV and gelatin (14).

Sets of genes enriched in DNA-related activities (e.g. DNA repair, cell cycle and telomere maintenance) and sets of genes involved in protein maintenance (e.g. unfolded protein binding, stress response, protein refolding and chaperones) appear in two sides in the analyzed bicliques (Supplementary Table S1).

According to the GO database the functional classifications of cell wall related; protein binding; stress response; ribosomal structural constituent; cytoplasmic biological processes; cellular component and other categories comprised 40.8% of all contigs with 3% (12/371) of the contigs linking directly with stress responses.

The PBR, which activates ING1 and ING2 by binding stress-induced phospholipids, overlaps with the UBD, resulting in competition between ubiquitin and phospholipids for binding of this region.

Colligin 2 (also known as CBP2 or heat shock protein 47) is a collagen-binding stress protein localized in the endoplasmic reticulum (14).

YB-1 and CSDA are two nucleic acid-binding stress proteins that contain a central cold-shock domain, a 100-amino acid sequence that derives its name from its resemblance to bacterial cold-shock proteins [ 38].

PerR regulates the expression of dps (DNA-binding stress protein, PputW610_4005), fur (the ferric uptake repressor, PputW619_0702), ahpCF and katA (Mongkolsuk & Helmann, 2002), all of which are present in P. Putida W619.

A search for sequence homology also revealed that a central region of the protein around residues 80 190 share low sequence homology 20-300% identity) to several highly helical proteins, including Vinculin (PDBID 1ST6) and DNA-binding stress response protein (2C2F).

Heat shock protein (HSP) 47 is a collagen-binding, stress-inducible protein localized to the endoplasmic reticulum.

The collagen-binding, stress-inducible protein, HSP47, acts as a collagen-specific molecular chaperone in the intracellular processing of procollagen [ 21- 23].

Heat shock protein (HSP) 47 is a collagen-binding, stress-inducible protein localized in the endoplasmic reticulum and is never released into the extracellular matrix.