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1 are similar to those of proteins containing HMG-box domains.
2 rotein HMGB1 contains two tandem DNA-binding HMG box domains, A and B, linked by a short flexible lin
3 omal protein with two homologous DNA-binding HMG-box domains, A and B, linked by a short basic region
4 of full-length HMGB1, containing two tandem HMG box domains and a C-terminal acidic tail, with cispl
5 ed within the extremities of the DNA-binding HMG-box domain and, although mutations within either cau
6 ty for all DNA substrates tested than single HMG-box domains and has a significantly higher ability t
8 h the transcription factor Lef-1 through its HMG-box domain as well as with other early development t
10 roteins are composed of one or two conserved HMG box domains, each forming three alpha-helices that f
13 urther supports the conclusion that only one HMG box domain is bound to the site of cisplatin damage.
14 a disprove the hypothesis that the conserved HMG box domain is the only functional domain of Sry, and
16 binding protein HMGB1 consists of two tandem HMG-box domains joined by a basic linker to a C-terminal
17 that contains mutations in residues of both HMG box domains known to affect DNA binding in vitro, an
19 mobility group B (HMGB) proteins contain two HMG box domains known to bind without sequence specifici
23 of 691 amino acids (72 kDa) and includes an HMG box domain, which is closely related to the mouse So