BIOMAT Database Logo BIOMAT Database Logo

Hydroxyl radical footprinting. 1991

W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius

UI MeSH Term Description Entries
D007202 Indicators and Reagents Substances used for the detection, identification, analysis, etc. of chemical, biological, or pathologic processes or conditions. Indicators are substances that change in physical appearance, e.g., color, at or approaching the endpoint of a chemical titration, e.g., on the passage between acidity and alkalinity. Reagents are substances used for the detection or determination of another substance by chemical or microscopical means, especially analysis. Types of reagents are precipitants, solvents, oxidizers, reducers, fluxes, and colorimetric reagents. (From Grant & Hackh's Chemical Dictionary, 5th ed, p301, p499) Indicator,Reagent,Reagents,Indicators,Reagents and Indicators
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009876 Operon In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION. Operons
D012097 Repressor Proteins Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release. Repressor Molecules,Transcriptional Silencing Factors,Proteins, Repressor,Silencing Factors, Transcriptional
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004268 DNA-Binding Proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D004279 DNA, Viral Deoxyribonucleic acid that makes up the genetic material of viruses. Viral DNA
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005609 Free Radicals Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. Free radicals include reactive oxygen and nitrogen species (RONS). They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated. Free Radical

Related Publications

W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Hydroxyl radical footprinting.
January 1994, Methods in molecular biology (Clifton, N.J.),
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Hydroxyl radical footprinting.
January 2001, Methods in molecular biology (Clifton, N.J.),
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Hydroxyl-radical footprinting.
December 2007, CSH protocols,
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
DNA footprinting with hydroxyl radical.
April 1988, Nature,
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
DNA footprinting with the hydroxyl radical.
January 1991, Free radical research communications,
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Probing RNA folding by hydroxyl radical footprinting.
January 2014, Methods in molecular biology (Clifton, N.J.),
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Hydroxyl radical footprinting of protein-DNA complexes.
January 2009, Methods in molecular biology (Clifton, N.J.),
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Identifying protein interactions by hydroxyl-radical protein footprinting.
November 2004, Current protocols in protein science,
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Mapping RNA-protein interactions using hydroxyl-radical footprinting.
December 2014, Cold Spring Harbor protocols,
W J Dixon, and J J Hayes, and J R Levin, and M F Weidner, and B A Dombroski, and T D Tullius
Chemical Generation of Hydroxyl Radical for Oxidative 'Footprinting'.
January 2019, Protein and peptide letters,
Copied contents to your clipboard!