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Results: 1 to 10 of 66

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Metabolic plasticity meets gene regulation.
Paudel BB, Quaranta V
(2019) Proc Natl Acad Sci U S A 116: 3370-3372
MeSH Terms: Biochemical Phenomena, Gene Expression Regulation, Humans, Metabolic Networks and Pathways, Neoplasms, Neuronal Plasticity
Added March 23, 2019
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2 Members
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6 MeSH Terms
Ion mobility-mass spectrometry strategies for untargeted systems, synthetic, and chemical biology.
May JC, Goodwin CR, McLean JA
(2015) Curr Opin Biotechnol 31: 117-21
MeSH Terms: Biochemical Phenomena, Humans, Ions, Mass Spectrometry
Show Abstract · Added December 17, 2018
Contemporary strategies that concentrate on only one or a handful of molecular targets limits the utility of the information gained for diagnostic and predictive purposes. Recent advances in the sensitivity, speed, and precision of measurements obtained from ion mobility coupled to mass spectrometry (IM-MS) have accelerated the utility of IM-MS in untargeted, discovery-driven studies in biology. Perhaps most evident is the impact that such wide-scale discovery capabilities have yielded in the areas of systems, synthetic, and chemical biology, where the need for comprehensive, hypothesis-driving studies from multidimensional and unbiased data is required.
Copyright © 2014 Elsevier Ltd. All rights reserved.
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1 Members
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MeSH Terms
Amended safety assessment of dodecylbenzenesulfonate, decylbenzenesulfonate, and tridecylbenzenesulfonate salts as used in cosmetics.
Becker LC, Bergfeld WF, Belsito DV, Hill RA, Klaassen CD, Liebler DC, Marks JG, Shank RC, Slaga TJ, Snyder PW, Andersen FA
(2010) Int J Toxicol 29: 288S-305
MeSH Terms: Alkanesulfonic Acids, Animals, Benzenesulfonates, Chemical Phenomena, Consumer Product Safety, Cosmetics, Detergents, Dose-Response Relationship, Drug, Humans, Irritants, Mutagenicity Tests, Rabbits, Skin, Surface-Active Agents, Toxicity Tests, Acute, Toxicity Tests, Chronic
Show Abstract · Added March 20, 2014
Sodium dodecylbenzenesulfonate is one of a group of salts of alkylbenzene sulfonates used in cosmetics as surfactant-cleansing agents. Sodium dodecylbenzenesulfonate is soluble in water and partially soluble in alcohol, with dermal absorption dependent on pH. Dodecylbenzenesulfonate salts are not toxic in single-dose oral and dermal animal tests, and no systemic toxicities were observed in repeat-dose dermal animal studies. In dermal animal studies, no evidence of reproductive or developmental toxicity was reported. At 15% concentrations, sodium dodecylbenzenesulfonate was severely irritating to rabbit skin. The Cosmetic Ingredient Review Expert Panel concluded that the irritant properties of these ingredients are similar to those of other detergents, with severity dependent on concentration and pH. Products containing these ingredients should be formulated to ensure that the irritancy potential is minimized.
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16 MeSH Terms
Final amended safety assessment of hydroquinone as used in cosmetics.
Andersen FA, Bergfeld WF, Belsito DV, Hill RA, Klaassen CD, Liebler DC, Marks JG, Shank RC, Slaga TJ, Snyder PW
(2010) Int J Toxicol 29: 274S-87
MeSH Terms: Administration, Cutaneous, Animals, Antioxidants, Carcinogenicity Tests, Chemical Phenomena, Clinical Trials as Topic, Consumer Product Safety, Cosmetics, Dose-Response Relationship, Drug, Humans, Hydroquinones, Mutagenicity Tests, Polymerization, Skin, Toxicity Tests, Acute, Toxicity Tests, Chronic
Show Abstract · Added March 20, 2014
Hydroquinone is an aromatic compound that functions in cosmetics as an antioxidant, fragrance, reducing agent, or polymerization inhibitor. Hydroquinone is also used as a skin bleaching agent. Safety and toxicity information indicate that hydroquinone is dermally absorbed in humans from both aqueous and alcoholic formulations and is excreted mainly as the glucuronide or sulfate conjugates. Hydroquinone is associated with altered immune function in vitro and in vivo in animals and an increased incidence of renal tubule cell tumors and leukemia in F344 rats, but the relevance to humans is uncertain. Quantitatively, however, the use of hydroquinone in cosmetics is unlikely to result in renal neoplasia through this mode of action. Thus, hydroquinone is safe at concentrations of ≤1% in hair dyes and is safe for use in nail adhesives. Hydroquinone should not be used in other leave-on cosmetics.
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16 MeSH Terms
Final report of the Cosmetic Ingredient Review Expert Panel amended safety assessment of Calendula officinalis-derived cosmetic ingredients.
Andersen FA, Bergfeld WF, Belsito DV, Hill RA, Klaassen CD, Liebler DC, Marks JG, Shank RC, Slaga TJ, Snyder PW
(2010) Int J Toxicol 29: 221S-43
MeSH Terms: Animals, Calendula, Carcinogenicity Tests, Chemical Phenomena, Consumer Product Safety, Cosmetics, Dose-Response Relationship, Drug, Flowers, Humans, Irritants, Mutagenicity Tests, Plant Extracts, Toxicity Tests, Acute, Toxicity Tests, Chronic
Show Abstract · Added March 20, 2014
Calendula officinalis extract, C officinalis flower, C officinalis flower extract, C officinalis flower oil, and C officinalis seed oil are cosmetic ingredients derived from C officinalis. These ingredients may contain minerals, carbohydrates, lipids, phenolic acids, flavonoids, tannins, coumarins, sterols and steroids, monoterpenes, sesquiterpenes, triterpenes, tocopherols, quinones, amino acids, and resins. These ingredients were not significantly toxic in single-dose oral studies using animals. The absence of reproductive/developmental toxicity was inferred from repeat-dose studies of coriander oil, with a similar composition. Overall, these ingredients were not genotoxic. They also were not irritating, sensitizing, or photosensitizing in animal or clinical tests but may be mild ocular irritants. The Cosmetic Ingredient Review (CIR) Expert Panel concluded that these ingredients are safe for use in cosmetics in the practices of use and concentration given in this amended safety assessment.
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14 MeSH Terms
A sulfilimine bond identified in collagen IV.
Vanacore R, Ham AJ, Voehler M, Sanders CR, Conrads TP, Veenstra TD, Sharpless KB, Dawson PE, Hudson BG
(2009) Science 325: 1230-4
MeSH Terms: Amino Acid Sequence, Animals, Cattle, Chemical Phenomena, Collagen Type IV, Humans, Hydroxylysine, Mass Spectrometry, Methionine, Models, Molecular, Molecular Sequence Data, Nitrogen, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Multimerization, Protein Subunits, Sequence Alignment, Stress, Mechanical, Sulfur
Show Abstract · Added December 10, 2013
Collagen IV networks are ancient proteins of basement membranes that underlie epithelia in metazoa from sponge to human. The networks provide structural integrity to tissues and serve as ligands for integrin cell-surface receptors. They are assembled by oligomerization of triple-helical protomers and are covalently crosslinked, a key reinforcement that stabilizes networks. We used Fourier-transform ion cyclotron resonance mass spectrometry and nuclear magnetic resonance spectroscopy to show that a sulfilimine bond (-S=N-) crosslinks hydroxylysine-211 and methionine-93 of adjoining protomers, a bond not previously found in biomolecules. This bond, the nitrogen analog of a sulfoxide, appears to have arisen at the divergence of sponge and cnidaria, an adaptation of the extracellular matrix in response to mechanical stress in metazoan evolution.
1 Communities
3 Members
1 Resources
19 MeSH Terms
Accessing ns-micros side chain dynamics in ubiquitin with methyl RDCs.
Farès C, Lakomek NA, Walter KF, Frank BT, Meiler J, Becker S, Griesinger C
(2009) J Biomol NMR 45: 23-44
MeSH Terms: Algorithms, Amino Acids, Branched-Chain, Carbon Isotopes, Chemical Phenomena, Humans, Models, Chemical, Models, Molecular, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Reproducibility of Results, Solvents, Ubiquitin
Show Abstract · Added January 24, 2015
This study presents the first application of the model-free analysis (MFA) (Meiler in J Am Chem Soc 123:6098-6107, 2001; Lakomek in J Biomol NMR 34:101-115, 2006) to methyl group RDCs measured in 13 different alignment media in order to describe their supra-tau (c) dynamics in ubiquitin. Our results indicate that methyl groups vary from rigid to very mobile with good correlation to residue type, distance to backbone and solvent exposure, and that considerable additional dynamics are effective at rates slower than the correlation time tau (c). In fact, the average amplitude of motion expressed in terms of order parameters S (2) associated with the supra-tau (c) window brings evidence to the existence of fluctuations contributing as much additional mobility as those already present in the faster ps-ns time scale measured from relaxation data. Comparison to previous results on ubiquitin demonstrates that the RDC-derived order parameters are dominated both by rotameric interconversions and faster libration-type motions around equilibrium positions. They match best with those derived from a combined J-coupling and residual dipolar coupling approach (Chou in J Am Chem Soc 125:8959-8966, 2003) taking backbone motion into account. In order to appreciate the dynamic scale of side chains over the entire protein, the methyl group order parameters are compared to existing dynamic ensembles of ubiquitin. Of those recently published, the broadest one, namely the EROS ensemble (Lange in Science 320:1471-1475, 2008), fits the collection of methyl group order parameters presented here best. Last, we used the MFA-derived averaged spherical harmonics to perform highly-parameterized rotameric searches of the side chains conformation and find expanded rotamer distributions with excellent fit to our data. These rotamer distributions suggest the presence of concerted motions along the side chains.
1 Communities
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13 MeSH Terms
Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution.
Lange OF, Lakomek NA, Farès C, Schröder GF, Walter KF, Becker S, Meiler J, Grubmüller H, Griesinger C, de Groot BL
(2008) Science 320: 1471-5
MeSH Terms: Amino Acid Motifs, Animals, Anisotropy, Chemical Phenomena, Chemistry, Physical, Crystallography, X-Ray, Entropy, Kinetics, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Solutions, Ubiquitin, Xenopus laevis
Show Abstract · Added January 24, 2015
Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.
1 Communities
1 Members
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16 MeSH Terms
Impaired tricarboxylic acid cycle activity in mouse livers lacking cytosolic phosphoenolpyruvate carboxykinase.
Burgess SC, Hausler N, Merritt M, Jeffrey FM, Storey C, Milde A, Koshy S, Lindner J, Magnuson MA, Malloy CR, Sherry AD
(2004) J Biol Chem 279: 48941-9
MeSH Terms: Animals, Biochemical Phenomena, Biochemistry, Citric Acid Cycle, Cytosol, Food Deprivation, Glucose, Hydrogen, Kinetics, Liver, Magnetic Resonance Spectroscopy, Mice, Mice, Knockout, Mitochondria, Models, Biological, NAD, Oxidation-Reduction, Oxygen Consumption, Perfusion, Phosphoenolpyruvate Carboxykinase (GTP), Phosphorylation, Time Factors
Show Abstract · Added April 10, 2012
Liver-specific phosphoenolpyruvate carboxykinase (PEPCK) null mice, when fasted, maintain normal whole body glucose kinetics but develop dramatic hepatic steatosis. To identify the abnormalities of hepatic energy generation that lead to steatosis during fasting, we studied metabolic fluxes in livers lacking hepatic cytosolic PEPCK by NMR using 2H and 13C tracers. After a 4-h fast, glucose production from glycogenolysis and conversion of glycerol to glucose remains normal, whereas gluconeogenesis from tricarboxylic acid (TCA) cycle intermediates was nearly absent. Upon an extended 24-h fast, livers that lack PEPCK exhibit both 2-fold lower glucose production and oxygen consumption, compared with the controls, with all glucose production being derived only from glycerol. The mitochondrial reduction-oxidation (red-ox) state, as indicated by the NADH/NAD+ ratio, is 5-fold higher, and hepatic TCA cycle intermediate concentrations are dramatically increased in the PEPCK null livers. Consistent with this, flux through the TCA cycle and pyruvate cycling pathways is 10- and 40-fold lower, respectively. Disruption of hepatic cataplerosis due to loss of PEPCK leads to the accumulation of TCA cycle intermediates and a nearly complete blockage of gluconeogenesis from amino acids and lactate (an energy demanding process) but intact gluconeogenesis from glycerol (which contributes to net NADH production). Inhibition of the TCA cycle and fatty acid oxidation due to increased TCA cycle intermediate concentrations and reduced mitochondrial red-ox state lead to the development of steatosis.
1 Communities
2 Members
0 Resources
22 MeSH Terms
Quantitative observation of backbone disorder in native elastin.
Pometun MS, Chekmenev EY, Wittebort RJ
(2004) J Biol Chem 279: 7982-7
MeSH Terms: Animals, Cattle, Chemical Phenomena, Chemistry, Physical, Deuterium, Elasticity, Elastin, Magnetic Resonance Spectroscopy, Proline, Protein Structure, Secondary, Spectrum Analysis, Thermodynamics, Water
Show Abstract · Added March 5, 2014
Elastin is a key protein in soft tissue function and pathology. Establishing a structural basis for understanding its reversible elasticity has proven to be difficult. Complementary to structure is the important aspect of flexibility and disorder in elastin. We have used solid-state NMR methods to examine polypeptide and hydrate ordering in both elastic (hydrated) and brittle (dry) elastin fibers and conclude (i) that tightly bound waters are absent in both dry and hydrated elastin and (ii) that the backbone in the hydrated protein is highly disordered with large amplitude motions. The hydrate was studied by (2)H and (17)O NMR, and the polypeptide by (13)C and (2)H NMR. Using a two-dimensional (13)C MAS method, an upper limit of S < 0.1 was determined for the backbone carbonyl group order parameter in hydrated elastin. For comparison, S approximately approximately 0.9 in most proteins. The former result is substantiated by two additional observations: the absence of the characteristic (2)H spectrum for stationary amides and "solution-like" (13)C magic angle spinning spectra at 75 degrees C, at which the material retains elasticity. Comparison of the observed shifts with accepted values for alpha-helices, beta-sheets, or random coils indicates a random coil structure at all carbons. These conclusions are discussed in the context of known thermodynamic properties of elastin and, more generally, protein folding. Because coacervation is an entropy-driven process, it is enhanced by the observed backbone disorder, which, we suggest, is the result of high proline content. This view is supported by recent studies of recombinant elastin polypeptides with systematic proline substitutions.
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13 MeSH Terms