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Showing 1-30 of 35 results for "A4021" within Papers
Jarrod B French et al.
Biochemistry, 47(38), 10227-10239 (2008-08-30)
Sirtuins are NAD (+)-dependent enzymes that deacetylate a variety of cellular proteins and in some cases catalyze protein ADP-ribosyl transfer. The catalytic mechanism of deacetylation is proposed to involve an ADPR-peptidylimidate, whereas the mechanism of ADP-ribosyl transfer to proteins is
Isolation and characterization of an acetylated impurity in Escherichia coli-derived recombinant human interleukin-10 (IL-10) drug substance.
M N Pflumm et al.
Pharmaceutical research, 14(6), 833-836 (1997-06-01)
Xingyou Wan et al.
Cell death & disease, 11(8), 649-649 (2020-08-20)
The folate-coupled metabolic enzyme MTHFD2 (the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase) confers redox homeostasis and drives cancer cell proliferation and migration. Here, we show that MTHFD2 is hyperacetylated and lysine 88 is the critical acetylated site. SIRT3, the major deacetylase in mitochondria
A case of hyperlysinemia: biochemical and clinical observations.
M D Armstrong et al.
Pediatrics, 39(4), 546-554 (1967-04-01)
Nuttara Jamonnak et al.
Organic & biomolecular chemistry, 5(6), 892-896 (2007-03-07)
Through parallel studies on peptides containing N(epsilon)-methanesulfonyl-lysine or N(epsilon)-acetyl-lysine, N(epsilon)-methanesulfonyl-lysine as a replacement for N(epsilon)-acetyl-lysine was shown i) not to compromise the binding affinity for a bromodomain, ii) to confer resistance to human HDAC8 and SIRT1 (two distinct protein deacetylases)
Heinz Neumann et al.
Nature chemical biology, 4(4), 232-234 (2008-02-19)
N(epsilon)-acetylation of lysine (1) is a reversible post-translational modification with a regulatory role that rivals that of phosphorylation in eukaryotes. No general methods exist to synthesize proteins containing N(epsilon)-acetyllysine (2) at defined sites. Here we demonstrate the site-specific incorporation of
A Jasinskas et al.
Biochimica et biophysica acta, 1351(1-2), 168-180 (1997-03-20)
Histone acetylation is an extremely complex, reversible and specific process. In order to evaluate the importance of this modification for gene expression during sea urchin development, acetyl group turnover of histone lysine residues was blocked by sodium butyrate. The continuous
A PƤhler et al.
Chemical research in toxicology, 11(9), 995-1004 (1998-10-07)
Antibodies directed against chemical specific protein modifications are valuable tools to detect and comparatively quantify protein modifications. Both Nepsilon-(dichloroacetyl)-L-lysine and Nepsilon-(trichloroacety)l-L-lysine have been detected as modified amino acids in liver and kidneys of rats treated with perchloroethene (PER) after proteolysis.
V D Trivedi
The Italian journal of biochemistry, 46(2), 67-73 (1997-06-01)
In order to explore the role of buried lysine residues of bovine serum albumin (BSA) in its interaction with bromophenol blue (BPB), three acetylated derivatives of albumin namely: 90%, 100% and 10%/chiefly having modification of buried lysine residues) were prepared
Tim Baldensperger et al.
Scientific reports, 10(1), 7596-7596 (2020-05-07)
Enzymatic and non-enzymatic posttranslational protein modifications by oxidation, glycation and acylation are key regulatory mechanisms in hallmarks of aging like inflammation, altered epigenetics and decline in proteostasis. In this study a mouse cohort was used to monitor changes of posttranslational
H Schmidt et al.
Antonie van Leeuwenhoek, 62(4), 285-290 (1992-11-01)
A novel aminotransferase catalyzing the second step of lysine catabolism, the oxidative transamination of the alpha-group of N6-acetyllysine, was identified and characterized in the yeast Candida maltosa. The enzyme was strongly induced in cells grown on L-lysine as sole carbon
T Henle et al.
Zeitschrift fur Lebensmittel-Untersuchung und -Forschung, 198(1), 66-67 (1994-01-01)
After heating N alpha-acetyllysine and glucose for 4 h at 90 degrees C in the dry state and subsequent acid hydrolysis with 7.8 N HCl, preparative fractionation of the dihydrochlorides of furosine and pyridosine was achieved by cation-exchange chromatography. The
S L Hazen et al.
The Journal of biological chemistry, 273(9), 4997-5005 (1998-03-28)
We have recently demonstrated that neutrophils oxidize nearly all of the amino acids commonly found in plasma to a corresponding family of aldehydes in high yield. The reaction is mediated by hypochlorous acid (HOCl), the major oxidant generated by the
Yana Cen et al.
Journal of the American Chemical Society, 132(35), 12286-12298 (2010-08-20)
Sirtuins are protein-modifying enzymes distributed throughout all forms of life. These enzymes bind NAD(+), a universal metabolite, and react it with acetyllysine residues to effect deacetylation of protein side chains. This NAD(+)-dependent deacetylation reaction has been observed for sirtuin enzymes
Nuttara Jamonnak et al.
Bioorganic chemistry, 38(1), 17-25 (2009-11-17)
Peptides containing L-N(epsilon)-acetyl-lysine (L-AcK) or its side chain modified analogs were prepared and assayed using SIRT1, the prototypical human silent information regulator 2 (Sir2) enzyme. While previous studies showed that the side chain acetyl group of L-AcK can be extended
J A Cohn et al.
Archives of biochemistry and biophysics, 328(1), 158-164 (1996-04-01)
We have previously shown that incubation of the model protein glucose-6-phosphate dehydrogenase (Glu-6-PDH) from the bacterium Leuconostoc mesenteroides with 4-hydroxy-2-nonenal (HNE), a major product of lipid peroxidation, results in the formation of cross-linked protein. HNE-modified protein is resistant to proteolytic
K Kawahara et al.
Biochemical and biophysical research communications, 266(2), 417-424 (1999-12-22)
Recent studies have implicated acetylation of several nuclear proteins such as histones and p53 on their epsilon-portion of lysine residues in eukaryotic transcription. Here we raised a specific polyclonal antibody against epsilon-acetylated lysine. Using the antibody, we detected hypernuclear acetylation
C Crane-Robinson et al.
Methods (San Diego, Calif.), 12(1), 48-56 (1997-05-01)
Acetylation of specific lysine residues in the N-terminal domains of core histones is a biochemical marker of active genes. To determine the spatial and temporal distribution of this reversible posttranslational modification, affinity-purified polyclonal antibodies recognizing the epitope epsilon-acetyllysine have been
Bahar Edrissi et al.
PLoS genetics, 9(2), e1003328-e1003328 (2013-03-08)
Aberrant protein modifications play an important role in the pathophysiology of many human diseases, in terms of both dysfunction of physiological modifications and the formation of pathological modifications by reaction of proteins with endogenous electrophiles. Recent studies have identified a
Ying Huang et al.
Molecular bioSystems, 6(4), 683-686 (2010-03-20)
By overexpressing the C-terminal domain of the ribosomal protein L11 to decrease release factor 1-mediated termination of protein translation, enhanced amber suppression is achieved in E. coli. This enhanced amber suppression efficiency allows the genetic incorporation of three N(epsilon)-acetyl-l-lysines into
D D Martin et al.
Biochimica et biophysica acta, 1524(1), 1-10 (2000-11-18)
Methanococcus thermolithotrophicus, a thermophilic methanogenic archaeon, produces and accumulates beta-glutamate and L-alpha-glutamate as osmolytes when grown in media with <1 M NaCl. When the organism is adapted to grow in >1 M NaCl, a new zwitterionic solute, N(epsilon)-acetyl-beta-lysine, is synthesized
Morten B Trelle et al.
Analytical chemistry, 80(9), 3422-3430 (2008-03-15)
Tandem mass spectrometry (MS/MS) is a powerful tool for characterization of post-translationally modified proteins, including epsilon-N-acetyllysine-containing species. Previous reports indicate that epsilon-N-acetyllysine immonium ions are useful marker ions for peptides containing epsilon-N-acetyllysine, but the specificity and sensitivity of these ions
Yasuhiko Komatsu et al.
Journal of immunological methods, 272(1-2), 161-175 (2002-12-31)
By employing two different immunogens and two different antibody-screening strategies, we established four mouse hybridoma clones producing monoclonal antibodies against N epsilon -acetyllysine. Three different protocols were used in this study; i.e., mice were (1) immunized with an N epsilon
Brett M Hirsch et al.
Molecular bioSystems, 7(1), 16-28 (2010-09-16)
Silent information regulator 2 (Sir2) enzymes or sirtuins are a family of intracellular protein deacetylases that can catalyze the Ī²-nicotinamide adenine dinucleotide (Ī²-NAD(+))-dependent deacetylation of N(Īµ)-acetyl-lysine on protein substrates, with the formation of lysine N(Īµ)-deacetylated protein species and small molecule
K Hoffmann et al.
Die Pharmazie, 55(8), 601-606 (2000-09-16)
Inhibitors of histone deacetylase (HD) are of great potential as new drugs due to their ability to influence transcriptional regulation and to induce apoptosis or differentiation in cancer cells. So far only radioactive enzyme activity assays or in-vivo assays with
J M Macdonald et al.
The Journal of biological chemistry, 275(41), 31908-31913 (2000-07-25)
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type ubiquitin and of the UbH68N
Praveen Rajendran et al.
Cancer research, 79(5), 918-927 (2019-01-16)
There continues to be interest in targeting epigenetic "readers, writers, and erasers" for the treatment of cancer and other pathologies. However, a mechanistic understanding is frequently lacking for the synergy observed when combining deacetylase and bromodomain inhibitors. Here we identify
B P Hudson et al.
Journal of molecular biology, 304(3), 355-370 (2000-11-25)
The solution structure of the bromodomain from the human transcriptional coactivator GCN5 has been determined using NMR methods. The structure has a left-handed four-helix bundle topology, with two short additional helices in a long connecting loop. A hydrophobic groove and
Mayuko Koreishi et al.
Bioscience, biotechnology, and biochemistry, 69(10), 1914-1922 (2005-10-26)
A novel aminoacylase was purified to homogeneity from culture broth of Streptomyces mobaraensis, as evidenced by SDS-polyacrylamide gel electrophoresis (PAGE). The enzyme was a monomer with an approximate molecular mass of 100 kDa. The purified enzyme was inhibited by the
R H Jacobson et al.
Science (New York, N.Y.), 288(5470), 1422-1425 (2000-05-29)
TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem
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