Guanine Nucleotide Exchange Factors
Guanosine Triphosphate
Rho Guanine Nucleotide Exchange Factors
Guanosine Diphosphate
GTP-Binding Proteins
ras Guanine Nucleotide Exchange Factors
Guanylyl Imidodiphosphate
Guanosine 5'-O-(3-Thiotriphosphate)
Guanosine
Guanosine Monophosphate
Guanine Nucleotide Dissociation Inhibitors
Molecular Sequence Data
Guanine Nucleotide-Releasing Factor 2
ADP-Ribosylation Factors
DNA
Hypoxanthine Phosphoribosyltransferase
Base Sequence
DNA Adducts
Virulence Factors, Bordetella
IMP Dehydrogenase
Proto-Oncogene Proteins c-vav
Adenylate Cyclase
Pertussis Toxin
Azaguanine
ras-GRF1
ral Guanine Nucleotide Exchange Factor
Purines
cdc42 GTP-Binding Protein
Adenosine Diphosphate Ribose
Amino Acid Sequence
ADP-Ribosylation Factor 1
Hypoxanthines
rac1 GTP-Binding Protein
rho GTP-Binding Proteins
Nucleic Acid Conformation
rhoA GTP-Binding Protein
Protein Binding
Adenylate Cyclase Toxin
Pentosyltransferases
rac GTP-Binding Proteins
Mutation
Alkylation
Acyclovir
Cell Membrane
G-Quadruplexes
rho-Specific Guanine Nucleotide Dissociation Inhibitors
Binding Sites
Cholera Toxin
rap1 GTP-Binding Proteins
rap GTP-Binding Proteins
Models, Molecular
Signal Transduction
SOS1 Protein
Protein Structure, Tertiary
Base Pairing
Oligodeoxyribonucleotides
Enzyme Activation
Escherichia coli
Proto-Oncogene Proteins p21(ras)
Purine Nucleotides
Oligonucleotides
ras Proteins
Aflatoxin B1
Eukaryotic Initiation Factor-2B
rho Guanine Nucleotide Dissociation Inhibitor alpha
Nucleotides
Transducin
Xanthopterin
ral GTP-Binding Proteins
Cattle
Magnesium
rab GTP-Binding Proteins
Proteins
Xanthine
Sequence Homology, Amino Acid
Nucleosides
Structure-Activity Relationship
Guanosine Diphosphate Sugars
N-Glycosyl Hydrolases
Substrate Specificity
Cloning, Molecular
O(6)-Methylguanine-DNA Methyltransferase
Hydrogen Bonding
Fluorides
DNA Damage
Inosine Monophosphate
Chromatography, High Pressure Liquid
DNA-Formamidopyrimidine Glycosylase
Macromolecular Substances
Nucleic Acid Denaturation
Heterotrimeric GTP-Binding Proteins
Brefeldin A
DNA Glycosylases
Monomeric GTP-Binding Proteins
COS Cells
Cyclic AMP
Transfection
GTP-Binding Protein alpha Subunits, G12-G13
Mutagens
Mutagenesis
Cells, Cultured
Phosphorylation
Molecular Structure
Recombinant Fusion Proteins
rab1 GTP-Binding Proteins
ras GTPase-Activating Proteins
Type C Phospholipases
GTP-Binding Protein alpha Subunits
rab5 GTP-Binding Proteins
Saccharomyces cerevisiae
Crystallography, X-Ray
Ribonucleotides
Receptors, Adrenergic, beta
DNA Repair
Adaptor Proteins, Signal Transducing
Binding, Competitive
Phosphatidylinositols
Colforsin
GTP-Binding Protein alpha Subunits, Gi-Go
Cross-Linking Reagents
Inositol Phosphates
Protein Conformation
Alkylating Agents
Mutagenesis, Site-Directed
Plasmids
Peptide Elongation Factor Tu
RNA
Inosine
HeLa Cells
7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide
Oncogene Protein p21(ras)
Eukaryotic Initiation Factor-2
Proto-Oncogene Proteins
Receptors, Cell Surface
Two-Hybrid System Techniques
Isoproterenol
Phosphoribosyl Pyrophosphate
Methylation
Magnetic Resonance Spectroscopy
Catalysis
Membrane Proteins
Oxidation-Reduction
Electrophoresis, Polyacrylamide Gel
Intercalating Agents
Point Mutation
Nucleic Acids
Antiviral Agents
Nucleoside Q
Carcinogens
Models, Biological
Ribonucleosides
DNA-Directed DNA Polymerase
Temperature
Epoxy Compounds
3T3 Cells
Cell Cycle Proteins
Liver
Thioguanine
Methylthioinosine
GTP-Binding Protein alpha Subunits, Gs
Aflatoxins
Protein Transport
Phosphoinositide Phospholipase C
p21-Activated Kinases
Carrier Proteins
Sequence Alignment
Saccharomyces cerevisiae Proteins
Ganciclovir
Turkeys
ran GTP-Binding Protein
Calcium
Cricetinae
Rod Cell Outer Segment
Long-range oxidative damage to DNA: effects of distance and sequence. (1/3529)
INTRODUCTION: Oxidative damage to DNA in vivo can lead to mutations and cancer. DNA damage and repair studies have not yet revealed whether permanent oxidative lesions are generated by charges migrating over long distances. Both photoexcited *Rh(III) and ground-state Ru(III) intercalators were previously shown to oxidize guanine bases from a remote site in oligonucleotide duplexes by DNA-mediated electron transfer. Here we examine much longer charge-transport distances and explore the sensitivity of the reaction to intervening sequences. RESULTS: Oxidative damage was examined in a series of DNA duplexes containing a pendant intercalating photooxidant. These studies revealed a shallow dependence on distance and no dependence on the phasing orientation of the oxidant relative to the site of damage, 5'-GG-3'. The intervening DNA sequence has a significant effect on the yield of guanine oxidation, however. Oxidation through multiple 5'-TA-3' steps is substantially diminished compared to through other base steps. We observed intraduplex guanine oxidation by tethered *Rh(III) and Ru(III) over a distance of 200 A. The distribution of oxidized guanine varied as a function of temperature between 5 and 35 degrees C, with an increase in the proportion of long-range damage (> 100 A) occurring at higher temperatures. CONCLUSIONS: Guanines are oxidized as a result of DNA-mediated charge transport over significant distances (e.g. 200 A). Although long-range charge transfer is dependent on distance, it appears to be modulated by intervening sequence and sequence-dependent dynamics. These discoveries hold important implications with respect to DNA damage in vivo. (+info)Regulation of de novo purine biosynthesis in human lymphoblasts. Coordinate control of proximal (rate-determining) steps and the inosinic acid branch point. (2/3529)
Purine nucleotide synthesis de novo has been studied in a permanent tissue culture line of human splenic lymphoblasts with particular attention to coordination of control of the proximal (rate-determining) steps with the distal branch point of the pathway. An assay was used which permits simultaneous determination of the overall rate of labeling of all intracellular purines with sodium [14C]formate, as well as the distribution of isotope into all intracellular guanine- and adenine-containing compounds. The guanine to adenine labeling ratio was used as an index of IMP branch point regulation. It was found that exogenous adenine and guanine produce feedback-controlling effects not only on the first step in the de novo pathway, but also on the IMP branch point. Concentrations of adenine which produce less than 40% inhibition of the overall rate of de novo purine synthesis do so by selectively inhibiting adenine nucleotide synthesis de novo by 50 to 70% while stimulating guanine nucleotide synthesis de novo by up to 20%. A reciprocal effect is seen with exogenous guanine. The adenosine analog 6-methylmercaptopurine ribonucleoside selectivity inhibits adenine nucleotide synthesis via the de novo pathway but not from exogenous hypoxanthine. Thus, the reactions of purine nucleotide interconversion, in particular adenylosuccinate synthetase, may be regulated differently in cells deriving their purine nucleotides solely from de novo synthesis than when deriving them via "salvage" of preformed hypoxanthine. (+info)The effect of cotinine or cigarette smoke co-administration on the formation of O6-methylguanine adducts in the lung and liver of A/J mice treated with 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) (3/3529)
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK), a tobacco-specific nitrosamine, induces lung adenomas in A/J mice, following a single intraperitoneal (i.p.) injection. However, inhalation of tobacco smoke has not induced or promoted tumors in these mice. NNK-induced lung tumorigenesis is thought to involve O6-methylguanine (O6MeG) formation, leading to GC-->AT transitional mispairing and an activation of the K-ras proto-oncogene in the A/J mouse. NNK can be metabolized by several different cytochromes P450, resulting in a number of metabolites. Formation of the promutagenic DNA adduct O6MeG is believed to require metabolic activation of NNK by cytochrome P450-mediated alpha-hydroxylation of the methylene group adjacent to the N-nitroso nitrogen to yield the unstable intermediate, methanediazohydroxide. Nicotine, cotinine (the major metabolite of nicotine), and aqueous cigarette tar extract (ACTE) have all been shown to effectively inhibit metabolic activation of NNK to its mutagenic form, most likely due to competitive inhibition of the cytochrome P450 enzymes involved in alpha-hydroxylation of NNK. The objective of the current study was to monitor the effects of cotinine and cigarette smoke (CS) on the formation of O6MeG in target tissues of mice during the acute phase of NNK treatment. To test the effect of cotinine, mature female A/J mice received a single intraperitoneal injection of NNK (0, 2.5, 5, 7.5, or 10 mumole/mouse) with cotinine administered at a total dose of 50 mumole/mouse in 3 separate i.p. injections, administered 30 min before, immediately after, and 30 min after NNK treatment. To test the effect of whole smoke exposure on NNK-related O6MeG formation, mice were exposed to smoke generated from Kentucky 1R4F reference cigarettes at 0, 0.4, 0.6, or 0.8 mg wet total particulate matter/liter (WTPM/L) for 2 h, with a single i.p. injection of NNK (0, 3.75, or 7.5 mumole/mouse) midway through the exposure. Cigarette smoke alone failed to yield detectable levels of O6MeG. The number of O6MeG adducts following i.p. injection of NNK was significantly (p < 0.05) reduced in both lung and liver by cotinine and by cigarette smoke exposure. Our results demonstrate that NNK-induced O6MeG DNA adducts in A/J mice are significantly reduced when NNK is administered together with either cotinine, the major metabolite of nicotine, or the parental complex mixture, cigarette smoke. (+info)Comparative study of the anti-human cytomegalovirus activities and toxicities of a tetrahydrofuran phosphonate analogue of guanosine and cidofovir. (4/3529)
Cidofovir is the first nucleoside monophosphate analogue currently being used for the treatment of human cytomegalovirus (HCMV) retinitis in individuals with AIDS. Unfortunately, the period of therapy with the use of this compound may be limited due to the possible emergence of serious irreversible nephrotoxic effects. New drugs with improved toxicity profiles are needed. The goal of this study was to investigate the anticytomegaloviral properties and drug-induced toxicity of a novel phosphonate analogue, namely, (-)-2-(R)-dihydroxyphosphinoyl-5-(S)-(guanin-9'-yl-methyl) tetrahydrofuran (compound 1), in comparison with those of cidofovir. The inhibitory activities of both compounds on HCMV propagation in vitro were similar against the AD 169 and Towne strains, with 50% inhibitory concentrations ranging from 0.02 to 0.17 microgram/ml for cidofovir and < 0.05 to 0.09 microgram/ml for compound 1. A clinical HCMV isolate that was resistant to ganciclovir and that had a known mutation within the UL54 DNA polymerase gene and a cidofovir-resistant laboratory strain derived from strain AD 169 remained sensitive to compound 1, whereas their susceptibilities to ganciclovir and cidofovir were reduced by 33- and 10-fold, respectively. Both compound 1 and cidofovir exhibited equal potencies in an experimentally induced murine cytomegalovirus (MCMV) infection in mice, with a prevention or prolongation of mean day to death at dosages of 1.0, 3.2, and 10.0 mg/kg of body weight/day. In cytotoxicity experiments, compound 1 was found to be generally more toxic than cidofovir in cell lines Hs68, HFF, and 3T3-L1 (which are permissive for HCMV or MCMV replication) but less toxic than cidofovir in MRC-5 cells (which are permissive for HCMV replication). Drug-induced toxic side effects were noticed for both compounds in rats and guinea pigs in a 5-day repeated-dose study. In guinea pigs, a greater weight loss was noticed with cidofovir than with compound 1 at dosages of 3.0 and 10.0 mg/kg/day. An opposite effect was detected in rats, which were treated with the compounds at relatively high dosages (up to 100 mg/kg/day). Compound 1 and cidofovir were nephrotoxic in both rats and guinea pigs, with the epithelium lining the proximal convoluted tubules in the renal cortex being the primary target site. The incidence and the severity of the lesions were found to be dose dependent. The lesions observed were characterized by cytoplasm degeneration and nuclear modifications such as karyomegaly, the presence of pseudoinclusions, apoptosis, and degenerative changes. In the guinea pig model, a greater incidence and severity of lesions were observed for cidofovir than for compound 1 (P < 0.001) with a drug regimen of 10 mg/kg/day. (+info)Mismatch repair and differential sensitivity of mouse and human cells to methylating agents. (5/3529)
The long-patch mismatch repair pathway contributes to the cytotoxic effect of methylating agents and loss of this pathway confers tolerance to DNA methylation damage. Two methylation-tolerant mouse cell lines were identified and were shown to be defective in the MSH2 protein by in vitro mismatch repair assay. A normal copy of the human MSH2 gene, introduced by transfer of human chromosome 2, reversed the methylation tolerance. These mismatch repair defective mouse cells together with a fibroblast cell line derived from an MSH2-/- mouse, were all as resistant to N-methyl-N-nitrosourea as repair-defective human cells. Although long-patch mismatch repair-defective human cells were 50- to 100-fold more resistant to methylating agents than repair-proficient cells, loss of the same pathway from mouse cells conferred only a 3-fold increase. This discrepancy was accounted for by the intrinsic N-methyl-N-nitrosourea resistance of normal or transformed mouse cells compared with human cells. The >20-fold differential resistance between mouse and human cells could not be explained by the levels of either DNA methylation damage or the repair enzyme O6-methylguanine-DNA methyltransferase. The resistance of mouse cells to N-methyl-N-nitrosourea was selective and no cross-resistance to unrelated DNA damaging agents was observed. Pathways of apoptosis were apparently intact and functional after exposure to either N-methyl-N-nitrosourea or ultraviolet light. Extracts of mouse cells were found to perform 2-fold less long-patch mismatch repair. The reduced level of mismatch repair may contribute to their lack of sensitivity to DNA methylation damage. (+info)The major, N2-dG adduct of (+)-anti-B[a]PDE induces G-->A mutations in a 5'-AGA-3' sequence context. (6/3529)
Previously, in a random mutagenesis study, the (+)-anti diol epoxide of benzo[a]pyrene [(+)-anti-B[a]PDE] was shown to induce a complex mutational spectrum in the supF gene of an Escherichia coli plasmid, which included insertions, deletions and base substitution mutations, notably a significant fraction of GC-->TA, GC-->AT and GC-->CG mutations. At some sites, a single type of mutation dominated and to understand individual mutagenic pathways these sites were chosen for study by site-specific means to determine whether the major adduct, [+ta]-B[a]P-N2-dG, was responsible. [+ta]-B[a]P-N2-dG was shown to induce approximately 95% G-->T mutations in a 5'-TGC-3' sequence context and approximately 80% G-->A mutations in a 5'-CGT-3' sequence context. (+)-anti-B[a]PDE induced principally GC-->CG mutations in the G133 sequence context (5'-AGA-3') in studies using both SOS-uninduced or SOS-induced E. coli. Herein, [+ta]-B[a]P-N2-dG is shown to induce principally G-->A mutations (>90%) either without or with SOS induction in a closely related 5'-AGA-3' sequence context (identical over 7 bp). This is the first time that there has been a discrepancy between the mutagenic specificity of (+)-anti-B[a]PDE versus [+ta]-B[a]P-N2-dG. Eight explanations for this discordance are considered. Four are ruled out; e.g. the second most prevalent adduct [+ca]-B[a]P-N2-dG also induces a preponderance of G-->A mutations (>90%), so it also is not responsible for (+)-anti-B[a]PDE-induced G133-->C mutations. The four explanations not ruled out are discussed and include that another minor adduct might be responsible and that the 5'-AGA-3' sequence context differed slightly in the studies with [+ta]-B[a]P-N2-dG versus (+)-anti-B[a]PDE. In spite of the discordance, [+ta]-B[a]P-N2-dG induces G-->A mutations in the context studied herein and this result has proven useful in generating a hypothesis for what conformations of [+ta]-B[a]P-N2-dG are responsible for G-->T versus G-->A mutations. (+info)In vitro reactions of butadiene monoxide with single- and double-stranded DNA: characterization and quantitation of several purine and pyrimidine adducts. (7/3529)
We have previously shown that butadiene monoxide (BM), the primary metabolite of 1,3-butadiene, reacted with nucleosides to form alkylation products that exhibited different rates of formation and different stabilities under in vitro physiological conditions. In the present study, BM was reacted with single-stranded (ss) and double-stranded (ds) calf thymus DNA and the alkylation products were characterized after enzymatic hydrolysis of the DNA. The primary products were regioisomeric N-7-guanine adducts. N-3-(2-hydroxy-3-buten-1-yl)adenine and N-3-(1-hydroxy-3-buten-2-yl)adenine, which were depurinated from the DNA more rapidly than the N-7-guanine adducts, were also formed. In addition, N6-(2-hydroxy-3-buten-1-yl)deoxyadenosine and N6-(1-hydroxy-3-buten-2-yl)deoxyadenosine were detected and evidence was obtained that these adducts were formed by Dimroth rearrangement of the corresponding N-1-deoxyadenosine adducts, not while in the DNA, but following the release of the N-1-alkylated nucleosides by enzymatic hydrolysis. N-3-(2-hydroxy-3-buten-1-yl)deoxyuridine adducts, which were apparently formed subsequent to deamination reactions of the corresponding deoxycytidine adducts, were also detected and were stable in the DNA. Adduct formation was linearly dependent upon BM concentration (10-1000 mM), with adduct ratios being similar at the various BM concentrations. At a high BM concentration (750 mM), the adducts were formed in a linear fashion for up to 8 h in both ssDNA and dsDNA. However, the rates of formation of the N-3-deoxyuridine and N6-deoxyadenosine adducts increased 10- to 20-fold in ssDNA versus dsDNA, whereas the N-7-guanine adducts increased only slightly, presumably due to differences in hydrogen bonding in ssDNA versus dsDNA. These results may contribute to a better understanding of the molecular mechanisms of mutagenesis and carcinogenesis of both BM and its parent compound, 1,3-butadiene. (+info)Identification of a C/G polymorphism in the promoter region of the BRCA1 gene and its use as a marker for rapid detection of promoter deletions. (8/3529)
Reduced expression of BRCA1 has been implicated in sporadic breast cancer, although the mechanisms underlying this phenomenon remain unclear. To determine whether regulatory mutations could account for the reduced expression, we screened the promoter region by sequencing in 20 patients with sporadic disease. No mutations were detected; however, a new polymorphism consisting of a C-to-G base change within the beta-promoter was identified, with the frequency of the G allele being 0.34. Close to complete linkage disequilibrium was found between this marker and the Pro871 Leu polymorphism, situated in exon 11, which has previously been shown not to be associated with breast or ovarian cancer. This indicates that the C/G polymorphism is also unlikely to play a role in either disease. However, the strength of linkage disequilibrium between these markers permitted their use for rapid screening for genomic deletions within BRCA1. A series of 214 cases with familial breast cancer were analysed using this approach; 88/214 were heterozygous for the promoter polymorphism, thereby excluding a deletion in this region. Among the remaining patients, one hemizygous case reflecting a promoter deletion was successfully identified. Therefore, this study indicates that deletions within the beta-promoter region of BRCA1 are an uncommon event in familial breast cancer. Furthermore, it suggests that mutations within the BRCA1 promoter are unlikely to account for the reported decreased expression of BRCA1 in sporadic disease. (+info)Term: Lesch-Nyhan Syndrome
Definition: A rare X-linked recessive genetic disorder caused by mutations in the HPRT1 gene, resulting in an impaired ability to metabolize uric acid and leading to symptoms such as gout, kidney stones, and other complications.
Etymology: Named after the physicians who first described the condition, Lesch and Nyhan.
Incidence: Approximately 1 in 165,000 male births.
Prevalence: Estimated to affect approximately 1 in 23,000 males worldwide.
Causes: Mutations in the HPRT1 gene, which codes for the enzyme hypoxanthine-guanine phosphoribosyltransferase (HPRT). This enzyme is involved in the metabolism of uric acid.
Symptoms: Gout attacks, kidney stones, joint pain and swelling, urate nephropathy (kidney damage), and other complications.
Diagnosis: Diagnosed through a combination of clinical evaluation, laboratory tests such as blood and urine analysis, and genetic testing to identify HPRT1 gene mutations.
Treatment: Medications to reduce uric acid levels, such as allopurinol or rasburicase, and management of symptoms such as pain and inflammation with nonsteroidal anti-inflammatory drugs (NSAIDs) or colchicine.
Prognosis: The condition is usually diagnosed in childhood, and patients often have a normal life expectancy if properly managed. However, untreated or poorly managed hyperuricemia can lead to complications such as kidney damage and cardiovascular disease.
Inheritance pattern: Autosomal recessive inheritance pattern, meaning that the individual must inherit two copies of the mutated HPRT1 gene (one from each parent) in order to develop the condition.
Other names: Hyperuricemia, gout, Lesch-Nyhan syndrome.
Guanine
Guanine deaminase
Guanine tetrad
Hypoxanthine-guanine phosphoribosyltransferase
Guanine-transporting ATPase
MRNA (guanine-N7-)-methyltransferase
TRNA (guanine-N1-)-methyltransferase
RRNA (guanine-N1-)-methyltransferase
TRNA (guanine-N7-)-methyltransferase
Guanine nucleotide exchange factor
TRNA (guanine-N2-)-methyltransferase
RRNA (guanine-N2-)-methyltransferase
EF1 guanine nucleotide exchange domain
Guano
Cisplatin
Classification of organic minerals
François Diederich
Nucleic acid structure
GNA15
DNA
GNA14
GMP synthase
GNAT3
Podoviridae
Nucleic acid analogue
Non-canonical base pairing
Nucleic acid structure determination
Base excision repair
RG9MTD2
GNA11
Guanine - New World Encyclopedia
NIOSHTIC-2 Publications Search - 00225420 - Fluorescence quantification of aflatoxin N7-guanine adducts.
ARHGEF2 Rho/Rac guanine nucleotide exchange factor 2 [Homo sapiens (human)] - Gene - NCBI
Mutations in the guanine nucleotide exchange factor gene IQSEC2 cause nonsyndromic intellectual disability
99mTc-Ethylenedicysteine-guanine - PubMed
Identification and Quantification of Aflatoxin Guanine and FapyGuanine Adducts in Mouse Liver invivo by LC-MS/MS Isotope...
Process for the preparation of pure guanine - Patent EP-0415028-B1 - PubChem
tRNA (guanine(6)-N2)-methyltransferase THUMP3 [Mus musculus] - Protein - NCBI
Vibrations of the guanine-cytosine pair in chloroform: an anharmonic computational study - Physical Chemistry Chemical Physics ...
RePub, Erasmus University Repository:
Expression of Concern: Guanine quadruplex structures localize to heterochromatin
INVESTIGATING THE CELLULAR IMPACT OF 8-OXO-GUANINE ON DNA REPLICATION AND GENOME STABILITY
Active cytomegalovirus particles in the eyes of an AIDS patient being treated with 9-[2-hydroxy-1-(hydroxymethyl) ethoxymethyl]...
Oxidized guanine lesions and hOgg1 activity in lung cancer.
The guanine exchange factor SWAP70 mediates vGPCR-induced endothelial plasticity - Inserm - Institut national de la santé et...
guanine - NIH Director's Blog
Subjects: Guanine Nucleotides - Digital Collections - National Library of Medicine Search Results
The Structural Duality of Nucleobases in Guanine Quadruplexes Controls Their Low-Energy Photoionization - CEA - Commissariat à...
DNA Guanine XX Round - DNA Diamonds
METTL1: tRNA (guanine-N(7)-)-methyltransferase
Rho Guanine Nucleotide Exchange Factors | Profiles RNS
DNA Guanine - Nucleobase 3D model by yas45 | 3DOcean
Changes related to "Guanine" - The School of Biomedical Sciences Wiki
Changes related to "Guanine" - The School of Biomedical Sciences Wiki
The significance of the metal cation in guanine-quartet - metalloporphyrin complexes
Guanine nucleotide-binding protein 2, GNBP2, accelerates the progression of clear cell renal cell carcinoma via regulation of...
CD2 antigen mediated activation of the guanine nucleotide binding proteins p21(ras) in human T lymphocytes<...
Susceptibility of the beta subunit of guanine nucleotide binding coupling proteins (G) to proteolytic cleavage<...
"The Eukaryotic Translation Elongation Factor 1Bγ Has a Non-guanine Nuc" by Anthony M. Esposito and Terri Goss Kinzy
Diversity in Guanine-Selective DNA Binding Modes for an Organometallic Ruthenium Arene Complex - Fingerprint - the UWA...
Nucleotides2
Cytosine4
- Guanine and adenine are derived from the two-ring parent molecule purine , and cytosine, thymine, and uracil are derived from the one-ring parent molecule pyrimidine . (newworldencyclopedia.org)
- In DNA, guanine and adenine form hydrogen bonds with their complementary pyrimidine derivatives, cytosine and thymine. (newworldencyclopedia.org)
- Thus, guanine, along with adenine and cytosine, is present in both DNA and RNA, whereas thymine is usually seen only in DNA and uracil only in RNA. (newworldencyclopedia.org)
- Guanine binds to cytosine through three hydrogen bonds. (newworldencyclopedia.org)
Nucleotide Exchange Factors3
- Rho Guanine Nucleotide Exchange Factors" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ouhsc.edu)
- This graph shows the total number of publications written about "Rho Guanine Nucleotide Exchange Factors" by people in this website by year, and whether "Rho Guanine Nucleotide Exchange Factors" was a major or minor topic of these publications. (ouhsc.edu)
- Below are the most recent publications written about "Rho Guanine Nucleotide Exchange Factors" by people in Profiles. (ouhsc.edu)
Adenine3
- Guanine oxidizes more readily than adenine , the other purine-derivative base in DNA and RNA. (newworldencyclopedia.org)
- A Fischer-Tropsch synthesis can also be used to form guanine, along with adenine , uracil , and thymine . (newworldencyclopedia.org)
- In FA, the triplet repeat is guanine-adenine-adenine, or GAA. (nih.gov)
Proteins1
- A family of guanine nucleotide binding proteins (G-proteins) functions in transmembrane signalling as receptor-effector couplers. (elsevierpure.com)
Quadruplexes2
- Guanine quadruplexes are four-stranded DNA/RNA structures composed of a guanine core (vertically stacked guanine tetrads) and peripheral groups (dangling ends and/or loops). (archives-ouvertes.fr)
- PPG peptide nucleic acids that promote DNA guanine quadruplexes. (nih.gov)
Adducts2
TRNA1
- Predicted to enable tRNA (guanine) methyltransferase activity. (nih.gov)
Protein4
- Guanine nucleotide-binding protein 2, GNBP2, accelerates the progression of clear cell renal cell carcinoma via regulation of STAT3 signaling transduction pathway. (bvsalud.org)
- Guanine nucleotide - binding protein 2 (GNBP2) is a GTPase that has critical roles in host immunity and some types of cancer , but its function in clear cell renal cell carcinoma (ccRCC) is not fully understood. (bvsalud.org)
- 2010) The eukaryotic translation elongation factor 1B{gamma} has a non-guanine nucleotide exchange factor role in protein metabolism. (illinoisstate.edu)
- The GNAS gene provides instructions for making one component, the stimulatory alpha subunit, of a protein complex called a guanine nucleotide-binding protein (G protein). (medlineplus.gov)
Subunit1
- These strains show severe defects in vacuole morphology and defects related to the maturation of carboxypeptidase Y that is not dependent on the catalytic subunit of the eEF1B complex as a guanine nucleotide exchange factor. (illinoisstate.edu)
Nucleobases1
- Such a dual structural arrangement of the nucleobases favors their photoionization at energies significantly lower than the guanine ionization potential. (archives-ouvertes.fr)
Chromosomes1
- Each of the 46 chromosomes in a human and guanine (G) -- which are strung along ribbons of sugar- cell's nucleus bears thousands of genes. (nih.gov)
Molecule1
- In this contribution we analyzed complexes of a guanine quartet with a porphyrin molecule, magnesium porphyrin and calcium porphyrin. (ac.rs)
Abstract1
- article{ author = "Stanojević, Ana and Milovanović, Branislav and Stanković, Ivana and Etinski, Mihajlo and Petković, Milena", year = "2021", abstract = "The planarity and the appropriate size of the porphyrin ring make porphyrin derivatives ideal ligands for stacking to guanine quartets and they could thus be used as anti-cancer drugs. (ac.rs)
Factor1
- Here we show that a mutation of IQSEC2, encoding a guanine nucleotide exchange factor for the ADP-ribosylation factor family of small GTPases, caused this disorder. (nih.gov)
Structures1
- The optimized structures of the three systems revealed geometrical changes in the guanine quartet upon complexation: while stacking of porphyrin and magnesium porphyrin does not induce significant changes, calcium porphyrin considerably distorts the quartet's structure, which has significant implications for the binding properties among guanine molecules. (ac.rs)
Form4
- Guanine (C 5 H 5 N 5 O), comprises a six-carbon pyrimidine ring fused with a five-carbon imidazole ring to form a system stabilized by conjugated double bonds (the positions of the double bonds shift around the ring). (newworldencyclopedia.org)
- The guanine nucleoside (guanine bonded with a five-carbon sugar) is called guanosine and lacks only a phosphate to form a nucleotide . (newworldencyclopedia.org)
- Guanine has two tautomeric forms: the keto form (characterized by an attached OH group) and the enol form (characterized by an attached CH2 group). (newworldencyclopedia.org)
- Trace amounts of guanine form by the polymerization of ammonium cyanide (NH 4 CN). (newworldencyclopedia.org)
Activity1
- Oxidized guanine lesions and hOgg1 activity in lung cancer. (nih.gov)
Deficiency3
- Complete deficiency of hypoxanthine-guanine phosphoribosyltransferase (HPRT) activity causes Lesch Nyhan disease (LND), characterized by hyperuricemia, severe action dystonia, choreoathetosis, ballismus, cognitive and attention deficit and self-injurious behavior. (nih.gov)
- Hypoxanthine-Guanine Phosphoribosyl-Transferase Deficiency: Avoid use of mycophenolate mofetil. (nih.gov)
- A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. (medlineplus.gov)
Adenine1
- In FA, the triplet repeat is guanine-adenine-adenine, or GAA. (nih.gov)
Hypoxanthine1
- Hypoxanthine-guanine phosphoribosyl transferase regulates early developmental programming of dopamine neurons: implications for Lesch-Nyhan disease pathogenesis. (nih.gov)
Active1
- Synthetic guanine derivative active against CMV. (medscape.com)
Human1
- Each of the 46 chromosomes in a human and guanine (G) -- which are strung along ribbons of sugar- cell's nucleus bears thousands of genes. (nih.gov)
Effects1
- Repair of O6-(2-chloroethyl)guanine mediates the biological effects of chloroethylnitrosoureas. (nih.gov)