BIOMAT Database Logo BIOMAT Database Logo

Signal transduction by guanine nucleotide-binding proteins: possible molecular basis for multiple forms of Go alpha mRNA. 1988

J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.

UI MeSH Term Description Entries
D009693 Nucleic Acid Hybridization Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503) Genomic Hybridization,Acid Hybridization, Nucleic,Acid Hybridizations, Nucleic,Genomic Hybridizations,Hybridization, Genomic,Hybridization, Nucleic Acid,Hybridizations, Genomic,Hybridizations, Nucleic Acid,Nucleic Acid Hybridizations
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
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
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D015246 Deoxyribonuclease EcoRI One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/AATTC at the slash. EcoRI is from E coliRY13. Several isoschizomers have been identified. EC 3.1.21.-. DNA Restriction Enzyme EcoRI,Deoxyribonuclease SsoI,Endonuclease EcoRI,Eco RI,Eco-RI,EcoRI Endonuclease,Endodeoxyribonuclease ECoRI,Endodeoxyribonuclease HsaI,Endonuclease Eco159I,Endonuclease Eco82I,Endonuclease RsrI,Endonuclease SsoI,HsaI Endonuclease,Restriction Endonuclease RsrI
D015247 Deoxyribonuclease HindIII One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence A/AGCTT at the slash. HindIII is from Haemophilus influenzae R(d). Numerous isoschizomers have been identified. EC 3.1.21.-. DNA Restriction Enzyme HindIII,Deoxyribonuclease BstFI,Deoxyribonuclease EcoVIII,Endonuclease HindIII,B Pertussis Restriction Enzyme I,BpeI Endonuclease,Endodeoxyribonuclease BpeI,Endonuclease Asp52I,Endonuclease BbrI,Endonuclease BpeI,Endonuclease BstFI,Endonuclease Cfr32I,Endonuclease ChuI,Endonuclease Eco65I,Endonuclease Eco98I,Endonuclease EcoVIII,Endonuclease Hin1076III,Endonuclease Hin173I,Endonuclease HinJCII,Endonuclease HinbIII,Endonuclease HinfII,Endonuclease HsuI,Endonuclease LlaCI,Endonuclease MkiI,LlaCI, Endonuclease
D015345 Oligonucleotide Probes Synthetic or natural oligonucleotides used in hybridization studies in order to identify and study specific nucleic acid fragments, e.g., DNA segments near or within a specific gene locus or gene. The probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the probe include the radioisotope labels 32P and 125I and the chemical label biotin. Oligodeoxyribonucleotide Probes,Oligonucleotide Probe,Oligoribonucleotide Probes,Probe, Oligonucleotide,Probes, Oligodeoxyribonucleotide,Probes, Oligonucleotide,Probes, Oligoribonucleotide
D015398 Signal Transduction The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal
D019204 GTP-Binding Proteins Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-. G-Proteins,GTP-Regulatory Proteins,Guanine Nucleotide Regulatory Proteins,G-Protein,GTP-Binding Protein,GTP-Regulatory Protein,Guanine Nucleotide Coupling Protein,G Protein,G Proteins,GTP Binding Protein,GTP Binding Proteins,GTP Regulatory Protein,GTP Regulatory Proteins,Protein, GTP-Binding,Protein, GTP-Regulatory,Proteins, GTP-Binding,Proteins, GTP-Regulatory

Related Publications

J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Signal transduction by guanine nucleotide binding proteins.
January 1987, Molecular and cellular endocrinology,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Signal transduction by guanine nucleotide-binding proteins.
January 1988, Recent progress in hormone research,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Guanine nucleotide binding proteins and signal transduction.
January 1988, Vitamins and hormones,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Guanine nucleotide regulatory proteins and signal transduction in the CNS--multiple mechanisms.
January 1986, Clinical neuropharmacology,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Factors determining the specificity of signal transduction by guanine nucleotide-binding protein-coupled receptors. II. Preferential coupling of the alpha 2C-adrenergic receptor to the guanine nucleotide-binding protein, Go.
May 1992, The Journal of biological chemistry,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Multiple alpha subunits of guanine nucleotide-binding proteins in Dictyostelium.
July 1989, Proceedings of the National Academy of Sciences of the United States of America,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.
June 2015, Science (New York, N.Y.),
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Multiple small molecular weight guanine nucleotide-binding proteins in human erythrocyte membranes.
February 1990, Biochemical and biophysical research communications,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
Molecular cloning and DNA sequence analysis of the human guanine nucleotide-binding protein Go alpha.
January 1988, Biochemical and biophysical research communications,
J J Murtagh, and S R Price, and K P Van Meurs, and C W Angus, and J Moss, and M Vaughan
ADP-ribosylation of signal-transducing guanine nucleotide-binding proteins by pertussis toxin.
January 1992, Current topics in microbiology and immunology,
Copied contents to your clipboard!