HMG1 and 2, and related 'architectural' DNA-binding proteins.
By Jean O. Thomas, A. Travers. TIBS -Trends in Biochemical Sciences. Regular ed, 2001
625 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5fd79ad6d32e295007dbd5e2c4a3b18e20b495f2
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In Molecular Biology
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Citations in the corpus
- The high mobility group protein HMG20A cooperates with the histone reader PHF14 to modulate TGFβ and Hippo pathways (2022, background): “Alpha helices 1, 2 and 3 display the typical ‘L’-shaped fold of the HMG box (35) (Figure 1B, Supplementary Figure S1B, C).”
- Linking biogeography to physiology: Evolutionary and acclimatory adjustments of thermal limits (2005, background): “High mobility group proteins are DNAbinding proteins that exert wide-ranging effects on transcriptional activity [30].”
- The Major Architects of Chromatin: Architectural Proteins in Bacteria, Archaea and Eukaryotes (2008, background): “HMG box domains are found in a wide variety of proteins that are capable of bending DNA (Thomas and Travers, 2001).”
- Androgen receptor (AR) coregulators: an overview. (2002, background): “Higher order DNA packaging is mediated by DNA architectural proteins, and the largest eukaryotic family of architectural proteins is the high-mobility group (HMG) proteins (211).”
- High‐mobility group box 1 (HMGB1) protein at the crossroads between innate and adaptive immunity (2007, background): “HMGB1 consists of two fairly rigid, L-shaped DNA-binding domains, each referred to as an ‘HMG box’ (10), and an unstructured tail that ends with 30 consecutive negatively charged amino acids (Fig.”
- The General Transcription Machinery and General Cofactors (2006, background): “Boxes A and B each forms an “L”-shaped structure with three α-helices constituting a minorgroove DNA-binding domain that preferentially binds distorted DNA, such as four-way junctions, cisplatinmodified DNA and bulged DNA, and induces DNA bending without sequence specificity (Thomas, 2001; Thomas an”
- Studies of the mitochondrial helicase Hmi1p in Candida albicans and Saccharomyces cerevisiae (2007, background): “function in DNA packaging into nucleoprotein complexes (Thomas and Travers, 2001).”