Photochemical cross-linking between proteins and nucleic acids as a probe of nucleoprotein interactions. 1980

R Sperling, and A Havron, and J Sperling

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009696 Nucleic Acids High molecular weight polymers containing a mixture of purine and pyrimidine nucleotides chained together by ribose or deoxyribose linkages. Nucleic Acid,Acid, Nucleic,Acids, Nucleic
D009698 Nucleoproteins Proteins conjugated with nucleic acids. Nucleoprotein
D009707 Nucleosomes The repeating structural units of chromatin, each consisting of approximately 200 base pairs of DNA wound around a protein core. This core is composed of the histones H2A, H2B, H3, and H4. Dinucleosomes,Polynucleosomes,Dinucleosome,Nucleosome,Polynucleosome
D010777 Photochemistry A branch of physical chemistry which studies chemical reactions, isomerization and physical behavior that may occur under the influence of visible and/or ultraviolet light. Photochemistries
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
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
D006657 Histones Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each. Histone,Histone H1,Histone H1(s),Histone H2a,Histone H2b,Histone H3,Histone H3.3,Histone H4,Histone H5,Histone H7
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

R Sperling, and A Havron, and J Sperling
January 1984, FEBS letters,
R Sperling, and A Havron, and J Sperling
January 1985, Seikagaku. The Journal of Japanese Biochemical Society,
R Sperling, and A Havron, and J Sperling
January 2002, Mass spectrometry reviews,
R Sperling, and A Havron, and J Sperling
August 1994, European journal of biochemistry,
R Sperling, and A Havron, and J Sperling
August 1956, Archives of biochemistry and biophysics,
R Sperling, and A Havron, and J Sperling
January 2008, Methods in molecular biology (Clifton, N.J.),
R Sperling, and A Havron, and J Sperling
January 1977, Biochimie,
R Sperling, and A Havron, and J Sperling
May 2017, Chemistry (Weinheim an der Bergstrasse, Germany),
R Sperling, and A Havron, and J Sperling
January 1997, Critical reviews in biochemistry and molecular biology,
Copied contents to your clipboard!