FR900482 class of anti-tumor drugs cross-links oncoprotein HMG I/Y to DNA in vivo
TLDR
Covalent cross-linking of DNA to HMG I/Y by FR900482 in vivo is reported which represents the first example of a covalent DNA-drug-protein cross-link with a minor groove-binding oncoprotein and a potential novel mechanism through which these compounds exert their anti-tumor activity.About:
This article is published in Chemistry & Biology.The article was published on 2000-10-01 and is currently open access. It has received 50 citations till now. The article focuses on the topics: Chromatin & HMG-box.read more
Citations
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Journal ArticleDOI
Molecular biology of HMGA proteins: hubs of nuclear function.
TL;DR: Recent advances that have contributed to the understanding of how this constellation of structural and biological features allows the HMGA proteins to serve as central 'hubs' of nuclear function are covered.
Journal ArticleDOI
HMGI/Y proteins: flexible regulators of transcription and chromatin structure.
Raymond Reeves,Lois Beckerbauer +1 more
TL;DR: It may well be that the inherent flexibility of the HMGI/Y proteins, combined with their ability to undergo reversible disordered-to-ordered structural transitions, has been a significant factor in the evolutionary selection of these proteins for their functional role(s) in cells.
Journal ArticleDOI
Mechanisms of in situ activation for DNA-targeting antitumor agents.
Journal ArticleDOI
DNA–protein crosslinks: their induction, repair, and biological consequences
TL;DR: The emergence of proteomics as a tool for identifying specific proteins that become crosslinked to DNA has heralded a new era in the ability to study DNA-protein crosslinks, and the identification of specific proteins cross linked to DNA should facilitate understanding of the down-stream effects of these lesions.
Journal ArticleDOI
Nuclear phosphoproteins HMGA and their relationship with chromatin structure and cancer
Riccardo Sgarra,Alessandra Rustighi,Michela A. Tessari,Julie Di Bernardo,Sandro Altamura,Alfredo Fusco,Guidalberto Manfioletti,Vincenzo Giancotti +7 more
TL;DR: The structural characteristics of the three nuclear phosphoproteins of the high mobility group A family are outlined and related to their participation in chromatin structure alteration in many biological processes such as gene expression, neoplastic transformation, differentiation, and apoptosis are outlined.
References
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Journal ArticleDOI
Virus induction of human IFNβ gene expression requires the assembly of an enhanceosome
Dimitris Thanos,Tom Maniatis +1 more
TL;DR: Evidence that transcriptional activation of the human interferon-beta (IFN beta) gene requires the assembly of a higher order transcription enhancer complex (enhanceosome) is presented and HMG I(Y) plays an essential role in the assembly and function of the IFN beta gene enhanceosome.
Journal ArticleDOI
Alu repeats and human disease.
TL;DR: Between these different mechanisms, Alu elements have not only contributed a great deal to the evolution of the genome but also continue to contribute to a significant portion of human genetic diseases.
Journal ArticleDOI
Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins.
TL;DR: All the HMG proteins are considered to function as architectural elements that modify the structure of DNA and chromatin to generate a conformation that facilitates and enhances various DNA-dependent activities.
Journal ArticleDOI
HMG domain proteins: architectural elements in the assembly of nucleoprotein structures
TL;DR: DNA bending induced by the H MG domain can facilitate the formation of higher-order nucleoprotein complexes, suggesting that HMG domain proteins may have an architectural role in assembling such complexes.
Book ChapterDOI
High-Mobility-Group Chromosomal Proteins: Architectural Components That Facilitate Chromatin Function
Michael Bustin,Raymond Reeves +1 more
TL;DR: This chapter summarizes recent information on the function of high-mobility-group (HMG) proteins and suggests that HMG proteins are associated with selected regions in chromatin and this association affects the architecture and increases the structural complexity of the chromatin fiber.
Related Papers (5)
HMGI/Y proteins: flexible regulators of transcription and chromatin structure.
Raymond Reeves,Lois Beckerbauer +1 more
The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure.
Raymond Reeves,Mark S. Nissen +1 more