Results 111 to 120 of about 2,248 (159)

Cisplatin ototoxicity to the rat inner ear: A role for HMG1 and iNOS

NeuroToxicology, 2006
Cisplatin is a chemotherapeutic agent that causes toxic damage to the inner ear (ototoxicity). Although much attention has been directed at identifying ways to protect the inner ear against cisplatin ototoxicity, little is known about the mechanisms by which cisplatin causes damage to the inner ear.
Geming, Li, Wei, Liu, Dorothy, Frenz
exaly   +3 more sources

The HMG1 Ta(i)le

Journal of Biomolecular Structure and Dynamics, 2002
We have studied structural changes in DNA/protein complexes using the CD spectroscopy, upon the interaction of HMG1-domains with calf thymus DNA at different ionic strengths. HMG1 protein isolated from calf thymus and recombinant HMG1-(A+B) protein were used. Recombinant protein HMG1-(A+B) represents a rat HMG1 lacking C-terminal acidic tail.
Alexander M. Polyanichko, Elena V. Chikhirzhina, Alexej N. Skvortsov, Elena I. Kostyleva, Pierre Colson, Claude Houssier, Vladimir I. Vorob'ev, Valery Ivanov   +7 more
openaire   +2 more sources

The chicken genome contains no HMG1 retropseudogenes but a functional HMG1 gene with long introns

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2000
We have cloned the genomic sequence coding for the high mobility group 1 (HMG1) protein in chickens. Multiple sequence alignment shows that the chicken HMG1 gene is highly homologous to the human and the mouse HMG1 genes. The gene structure of chicken HMG1 is similar to that of the mouse and the human HMG1 genes, with the same exon-intron boundaries ...
H K, Lum, K D, Lee, G, Yu
openaire   +2 more sources

HMG1 is not rearranged by 13q12 aberrations in lipomas

Genes, Chromosomes and Cancer, 1999
Several cytogenetic subgroups with characteristic lesions involving chromosomal regions 12q14-15, 6p21.3, or 13q12 can be distinguished in lipomas. Rearrangements of the HMGIC gene have been described in cases with 12q14-15 abnormalities, whereas HMGIY has been shown to be the target gene of 6p21.3 aberrations. Recently, HMG1, another member of the HMG
B, Kazmierczak, P, Dal Cin, K, Meyer-Bolte, H, Van den Berghe, J, Bullerdiek   +4 more
openaire   +2 more sources

HMG1 Domains: The Victims of the Circumstances

Molecular Biology, 2002
The method of circular dichroism (CD) was used to compare DNA behavior during its interaction with linker histone H1 and with nonhistone chromosomal protein HMG1 at different ionic strength and at different protein content in the system. The role of the negatively charged C-terminal segment of HMG1 was analyzed using recombinant protein HMG1-(A+B ...
E. V. Chikhirzhina, A. M. Polyanichko, A. N. Skvortsov, E. I. Kostyleva, C. Houssier, V. I. Vorob'ev   +5 more
openaire   +1 more source

Specific Recognition of Cruciform DNA by Nuclear Protein HMG1

Science, 1989
Cruciform DNA, a non-double helix form of DNA, can be generated as an intermediate in genetic recombination as well as from palindromic sequences under the effect of supercoiling. Eukaryotic cells are equipped with a DNA-binding protein that selectively recognizes cruciform DNA.
Bianchi M. E., Beltrame M., Paonessa G.
openaire   +3 more sources

HMG1 and 2, and related ‘architectural’ DNA-binding proteins

Trends in Biochemical Sciences, 2001
The HMG-box proteins, one of the three classes of high mobility group (HMG) chromosomal proteins, bend DNA and bind preferentially to distorted DNA structures. The proteins appear to act primarily as architectural facilitators in the assembly of nucleoprotein complexes; for example, in effecting recombination and in the initiation of transcription. HMG-
J O, Thomas, A A, Travers
openaire   +2 more sources

Structural requirements for cooperative binding of HMG1 to DNA minicircles

Journal of Molecular Biology, 2001
DNA minicircles, where the length of DNA is below the persistence length, are highly effective, preferred, ligands for HMG-box proteins. The proteins bind to them "structure-specifically" with affinities in the nanomolar range, presumably to an exposed widened minor groove.
M, Webb, D, Payet, K B, Lee, A A, Travers, J O, Thomas   +4 more
openaire   +2 more sources

Nuclear accumulation of HMG1 protein is correlated to DNA synthesis

Biology of the Cell, 1986
The subcellular localization of HMG1 protein was studied by immunoelectron microscopy during growth of CV1 cells in culture and in confluent CV1 cells subsequently lytically infected with SV40. HMG1 was always detected in the cytoplasm of both non‐infected and infected cells.
C, Bonne-Andrea, F, Harper, E, Puvion, M, Delpech, A M, De Recondo   +4 more
openaire   +2 more sources