Nothing Special   »   [go: up one dir, main page]

Patel et al., 1994 - Google Patents

Energy transfer analysis of Fos-Jun dimerization and DNA binding.

Patel et al., 1994

View PDF
Document ID
11132420557464062715
Author
Patel L
Curran T
Kerppola T
Publication year
Publication venue
Proceedings of the National Academy of Sciences

External Links

Snippet

The protooncogenes fos and jun encode proteins that bind to DNA as dimeric complexes and regulate gene expression. Protein dimerization is mediated by a leucine zipper and results in juxtaposition of regions of each protein rich in basic amino acids that comprise a …
Continue reading at www.pnas.org (PDF) (other versions)

Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay
    • G01N33/536—Immunoassay; Biospecific binding assay with immune complex formed in liquid phase
    • G01N33/542—Immunoassay; Biospecific binding assay with immune complex formed in liquid phase with steric inhibition or signal modification, e.g. fluorescent quenching
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay
    • G01N33/531—Production of immunochemical test materials
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
    • C12Q1/6813—Hybridisation assays
    • C12Q1/6816—Hybridisation assays characterised by the means of detection
    • C12Q1/6818—Hybridisation assays characterised by the means of detection involving interaction of at least two labels, e.g. resonant energy transfer
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used

Similar Documents

Publication Publication Date Title
Patel et al. Energy transfer analysis of Fos-Jun dimerization and DNA binding.
Matthews et al. A class of zinc fingers involved in protein–protein interactions: Biophysical characterization of CCHC fingers from Fog and U‐shaped
De Groot et al. Molecular insights into mammalian end-binding protein heterodimerization
JP6707472B2 (en) Tag that activates and shifts fluorophores (FAST)
Odom Jr et al. Distances between 3'ends of ribosomal ribonucleic acids reassembled into Escherichia coli ribosomes
US7329494B2 (en) Method of detection and quantification of cGMP by using a cGMP-visualizing probe
US6670144B1 (en) Compositions and methods for monitoring the phosphorylation of natural binding partners
US6808874B2 (en) Methods of monitoring enzyme activity
Huang et al. Characterization of the nucleotide binding properties of SV40 T antigen using fluorescent 3 ‘(2 ‘)-O-(2, 4, 6-trinitrophenyl) adenine nucleotide analogues
Graham et al. A method to measure the interaction of Rac/Cdc42 with their binding partners using fluorescence resonance energy transfer between mutants of green fluorescent protein
Bhattacharyya et al. A fluorescence spectroscopic study of glutaminyl‐tRNA synthetase from Escherichia coli and its implications for the enzyme mechanism
Ghetu et al. Probing FinO–FinP RNA interactions by site-directed protein–RNA crosslinking and gelFRET
Robbins et al. Position of transfer ribonucleic acid on Escherichia coli ribosomes. Distance from the 3'end of 16S ribonucleic acid to three points on phenylalanine-accepting transfer ribonucleic acid in the donor site of 70S ribosomes
EP1155321A1 (en) Compositions and methods for monitoring the modification of engineered binding partners
US20220169682A1 (en) Split photoactive yellow protein complementation system and uses thereof
Laham et al. Identification of two sites in gelsolin with different sensitivities to adenine nucleotides
Robbins et al. Comparison of ribosomal entry and acceptor transfer ribonucleic acid binding sites on Escherichia coli 70S ribosomes. Fluorescence energy transfer measurements from Phe-tRNAPhe to the 3'end of 16S ribonucleic acid
US20030162237A1 (en) Methods of monitoring enzyme activity
Bai et al. Interaction between bovine serum albumin and Indo-1 using fluorescence spectroscopic method
Krasitskaya et al. Development and Characterization of Novel DNA Aptamers Specific to Heart-Type Fatty Acid Binding Protein (hFABP)
Khrenova et al. Fluorescent proteins
GB2375538A (en) Polypeptide constructs for FRET analysis
US20030100037A1 (en) Chemical modification
Feng Functional Consequences of Physical Interactions Between PriA and PriB in DNA Replication Restart Pathways in Neisseria Gonorrhoeae
Millar Application of Time-Resolved Fluorescence Spectroscopy to Studies of DNA-Protein Interactions and RNA Folding