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1 alized by comparison of solved structures of HMGB proteins.
2 ecific and non-sequence-specific families of HMGB proteins.
3 tural factors such as high mobility group B (HMGB) proteins.
4 ctural proteins such as high mobility group (HMGB) proteins.
5 ively identified as high mobility group box (HMGB) proteins 1 and 3, and a 70-kDa band was identified
6 e chromatin protein high mobility group box (HMGB) protein 2 is restricted to the SZ in articular car
7 e chromatin protein high-mobility group box (HMGB) protein 2 is uniquely expressed in the superficial
9 E. coli cells to explore the extent to which HMGB proteins and derivatives can complement a DNA loopi
10 nds are only moderately discriminated by the HMGB proteins and TBP, but the recognition of dsTG*G*A i
12 HMO1 is one of 10 Saccharomyces cerevisiae HMGB proteins, and it is required for normal growth and
19 two eukaryotic high-mobility group class B (HMGB) proteins binding to approximately 200-bp DNA molec
20 ed proteins, of which high-mobility group B (HMGB) proteins consistently cofractionated by cation-exc
24 es for nucleosomes over linker DNA, and both HMGB proteins destabilize and unwind DNA from the H2A-H2
26 ic recognition of DNA kinks, we propose that HMGB proteins facilitate RAG1/2-RSS interactions by reco
28 ein is an essential high mobility group box (HMGB) protein facilitating Pol I transcription in T. bru
36 ows that linker histones and the chromosomal HMGB proteins, HMG-D and HMG-Z, have opposite effects on
37 show here that the Saccharomyces cerevisiae HMGB protein HMO1 stabilizes chromatin as evidenced by f
38 s features with the Saccharomyces cerevisiae HMGB protein Hmo1, but it is the first architectural chr
40 ker histone H1 and the functionally opposite HMGB proteins is critical for higher-order chromatin str
42 cterial DNA-binding protein HU and the yeast HMGB protein NHP6A display the same phenomenon of protei
43 ability of the abundant chromatin-associated HMGB protein Nhp6A from Saccharomyces cerevisiae to trav
44 Here, we show that derivatives of the yeast HMGB protein Nhp6A rescue DNA looping in E. coli lacking
47 Our observations support a model in which HMGB proteins soften DNA through random dynamic binding
49 eriments to show that high mobility group B (HMGB) proteins strongly disrupt nucleosomes, revealing a
51 (h-mtTFA) is a dual high mobility group box (HMGB) protein that binds site-specifically to the mitoch
52 results show that HMO1 shares with mammalian HMGB proteins the ability to promote DNA association.
53 ruits the family of high mobility group box (HMGB) proteins to chromatin along with the histone chape
54 linker histones and high-mobility group box (HMGB) proteins--to DDR and their potential significance
55 ne the nature of this behavior for different HMGB proteins, we used atomic force microscopy to quanti