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1 small DNA-binding domain first identified in high mobility group proteins.
2 ral similarity to the DNA-binding domains of high mobility group proteins.
3 chromatin-associated proteins histone H1 and high mobility group proteins.
4 " binding of the tandem A and B HMG boxes of high mobility group protein 1 (HMG1) to four-way junctio
5 xtension assays performed in the presence of high mobility group protein 1 (HMG1), which is known to
9 sequence analysis revealed that p30 was the high mobility group protein 1, which has been shown to f
11 ified by protein mass spectroscopy, included high mobility group proteins 1 and 2 (HMGB1, HMGB2), hea
13 We previously reported that the chromatin high-mobility group protein 1 (HMG-1) enhances the seque
19 the identification of 4 histone proteins, 4 high-mobility group proteins, 13 transcription factors,
21 that encodes an N-terminal fragment of human high mobility group protein 2 (HMGN2, formerly HMG-17).
22 itive component 4) coactivator but not HMG2 (high mobility group protein 2) and when the template is
23 th the chromatin structures of the host gene high mobility group protein A1 (HMGA1) and viral long te
30 ted the PDI-ELISA method using the mammalian high-mobility-group protein AT-hook 2 (HMGA2) as the pro
33 le of a chromatin-associated nuclear protein high mobility group protein B1 (HMGB1) in apoptotic resp
35 ctivity (toll-like receptor 4 expression and high mobility group protein B1 [HMGB-1] release) and nor
38 s-inducing factor (AIF), and proinflammatory high-mobility group protein B1 (HMGB-1) was effectively
41 , TLR4), which sense double-stranded RNA and high-mobility group protein B1 (HMGB1), respectively, as
42 ustaining, pathologic inflammation involving high-mobility group protein B1, interleukin-23, and the
43 neutrophil gelatinase-associated lipocalin, high-mobility group protein B1, intracellular cell adhes
45 eins, Ctcf (CCCTC-binding factor) and Hmgb2 (high mobility group protein B2), in regulating pathologi
46 ymphoid enhancer-binding factor (Lef) 1 is a high mobility group protein best known as a Wnt-responsi
47 mologue, vnd, interacts genetically with the high-mobility group protein, Dichaete, in a manner sugge
48 ory factor 1, and p50/p65 of NF-kappaB), the high mobility group protein HMG I(Y), and the correct al
50 hromatin protein-1 (HP1), histone H1 and the high mobility group protein HMG-I/Y are elevated at the
51 -downstream regions of the gene encoding the high mobility group protein HMG-I/Y from pea have been i
52 pression has been shown to interact with the high mobility group proteins HMG-1 and HMG-I/Y isolated
61 P2 motifs have overlapping binding sites for high mobility group proteins (HMG1+2), DNA-bending facto
65 Previously, we and others reported that the high mobility group proteins, HMGB-1/-2, enhance DNA bin
69 icates that the nucleosome binding family of high mobility group proteins (HMGN) facilitates the form
71 rRNA processing by regulating binding of the high mobility group protein Hmo1 and the small ribosomal
76 ular mechanism behind the involvement of the high mobility group protein I(Y) in interferon beta enha
78 s, we demonstrate that the overexpression of high mobility group protein I-C (HMGI-C), a Ras/ERK-indu
79 3) with stroke, and the LHFPL2 gene (lipoma high mobility group protein I-C fusion partner-like 2) w
80 and/or by the interaction of NF-kappaB with high-mobility group protein I (HMG I) on selected promot
81 eins, including E47/Pan1, BETA2/NeuroD1, and high-mobility group protein I(Y), to an activation compl
84 ce DNA lesions that are capable of retaining high mobility group proteins inside the nucleus of cells
85 NA-binding proteins, ribosomal proteins, and high-mobility group proteins is an evolutionarily conser
89 eractions between TBP and either Gcn5 or the high-mobility-group protein Nhp6, including multicopy su
90 ssembly and activity in vitro is promoted by high mobility group proteins of the "HMG-box" family, ex
92 sly shown that CK2 associates with the human high-mobility group protein SSRP1 and that this associat
93 /B (NHP6A/B) of Saccharomyces cerevisiae are high mobility group proteins that bind and severely bend
95 ion of binding of the murine testis-specific high-mobility group protein tsHMG to DNA modified by cis
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