WordNet
- matter that remains after something has been removed
- a colorless crystalline amino acid found in protein; occurs in the hydrolysates of certain proteins; an essential component of human nutrition
PrepTutorEJDIC
- 残り,残余;残留物
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- 1. III型遺伝性血管性浮腫 type iii hereditary angioedema
- 2. 複合免疫不全 combined immunodeficiencies
- 3. 正常ヒトヘモグロビンの構造および機能 structure and function of normal human hemoglobins
- 4. 成人におけるS状結腸鏡検査および大腸内視鏡検査のための前処置 bowel preparation for colonoscopy and flexible sigmoidoscopy in adults
- 5. ビタミンＫおよびγカルボキシグルタミン酸の合成 vitamin k and the synthesis of gamma carboxyglutamic acid
English Journal
- Human cytidine deaminase: A biochemical characterization of its naturally occurring variants.
- Micozzi D1, Carpi FM1, Pucciarelli S1, Polzonetti V1, Polidori P2, Vilar S3, Williams B4, Costanzi S5, Vincenzetti S6.Author information 1School of Biosciences and Biotechnology, University of Camerino, via Gentile III da Varano, 62032 Camerino, MC, Italy.2School of Pharmacy, University of Camerino, via circonvallazione 93/95, 62024 Matelica, MC, Italy.3Department of Organic Chemistry, Faculty of Pharmacy, University of Santiago de Compostela, Santiago de Compostela 15782, Spain.4Department of Chemistry, American University, Washington, DC 20016, USA.5Department of Chemistry, American University, Washington, DC 20016, USA. Electronic address: costanzi@american.edu.6School of Veterinary Medical Sciences, University of Camerino, via circonvallazione 93/95, 62024 Matelica, MC, Italy. Electronic address: silvia.vincenzetti@unicam.it.AbstractHuman cytidine deaminase is an enzyme of the pyrimidine salvage pathways that metabolizes several cytosine nucleoside analogs used as prodrugs in chemotherapy. We carried out a characterization of the cytidine deaminase 79A>C and 208G>A Single Nucleotide Polymorphisms, in order to highlight their functional role and provide data that could help fine-tune the chemotherapic use of cytosine nucleosides in patients carrying the above mentioned SNPs. The 79A>C SNP results in a K27Q change in a protein region not involved in the catalytic event. The 208G>A SNP produces an alanine to threonine substitution (A70T) within the conserved catalytic domain. Q27 variant is endowed with a greater catalytic efficiency toward the natural substrates and the antileukemic agent cytarabine (Ara-C), when compared to K27 variant. Molecular modeling, protein stability experiments and site-directed mutagenesis suggest that K27 variant may have an increased stability with respect to Q27 due to an ionic interaction between a lysine residue at position 27 and a glutamate residue at position 24. The T70 variant has a lower catalytic efficiency toward the analyzed substrates when compared to the A70 variant, suggesting that patients carrying the 208G>A SNP may have a greater exposure to cytosine based pro drugs, with possible toxicity consequences.
- International journal of biological macromolecules.Int J Biol Macromol.2014 Feb;63:64-74. doi: 10.1016/j.ijbiomac.2013.10.029. Epub 2013 Oct 29.
- Human cytidine deaminase is an enzyme of the pyrimidine salvage pathways that metabolizes several cytosine nucleoside analogs used as prodrugs in chemotherapy. We carried out a characterization of the cytidine deaminase 79A>C and 208G>A Single Nucleotide Polymorphisms, in order to highlight th
- PMID 24183806
- Depsipeptide substrates for sortase-mediated N-terminal protein ligation.
- Williamson DJ, Webb ME, Turnbull WB.Author information School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.AbstractTechnologies that allow the efficient chemical modification of proteins under mild conditions are widely sought after. Sortase-mediated peptide ligation provides a strategy for modifying the N or C terminus of proteins. This protocol describes the use of depsipeptide substrates (containing an ester linkage) with sortase A (SrtA) to completely modify proteins carrying a single N-terminal glycine residue under mild conditions in 4-6 h. The SrtA-mediated ligation reaction is reversible, so most labeling protocols that use this enzyme require a large excess of both substrate and sortase to produce high yields of ligation product. In contrast, switching to depsipeptide substrates effectively renders the reaction irreversible, allowing complete labeling of proteins with a small excess of substrate and catalytic quantities of sortase. Herein we describe the synthesis of depsipeptide substrates that contain an ester linkage between a threonine and glycolic acid residue and an N-terminal FITC fluorophore appended via a thiourea linkage. The synthesis of the depsipeptide substrate typically takes 2-3 d.
- Nature protocols.Nat Protoc.2014 Feb;9(2):253-62. doi: 10.1038/nprot.2014.003. Epub 2014 Jan 9.
- Technologies that allow the efficient chemical modification of proteins under mild conditions are widely sought after. Sortase-mediated peptide ligation provides a strategy for modifying the N or C terminus of proteins. This protocol describes the use of depsipeptide substrates (containing an ester
- PMID 24407354
- Identification of a novel mutation in the CLCN5 gene in a Chinese family with Dent-1 disease.
- Zhang H, Wang C, Yue H, Hu WW, Gu JM, He JW, Fu WZ, Liu YJ, Zhang Z, Zhang ZL.Author information Metabolic Bone Disease and Genetic Research Unit, Department of Osteoporosis and Bone Diseases, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai, China.AbstractDent disease comprises a group of X-linked recessive inherited renal tubular disorders, the symptoms of which include low-molecular-weight proteinuria (LMWP), hypercalciuria, nephrocalcinosis, and progressive renal failure. We sought to characterize the clinical manifestations and to identify the mutations associated with this disease in Chinese patients. In total, 155 DNA samples were collected from one affected individual, four of his family members, and 150 healthy donors. All 12 exons and the exon-intron boundaries of the CLCN5 gene were amplified and directly sequenced in this Chinese family. The proband demonstrated osteomalacia, which had resulted in more than 10 fractures, LMWP, and renal failure. A single base 'G' deletion at nucleotide 246 (c. 246delG) was identified in exon 5 of the CLCN5 gene in this patient, resulting in a frame shift mutation (fsX) that changed the Threonine (Thr) residue in position 83 to Proline (Pro). The proband's mother was found to be a carrier of this mutation. The present study suggests that a novel frameshift mutation (c. 246delG) in exon 5 of the CLCN5 gene is responsible for Dent disease in this case. Our findings also expand the known spectrum of CLCN5 mutations.
- Nephrology (Carlton, Vic.).Nephrology (Carlton).2014 Feb;19(2):80-3. doi: 10.1111/nep.12179.
- Dent disease comprises a group of X-linked recessive inherited renal tubular disorders, the symptoms of which include low-molecular-weight proteinuria (LMWP), hypercalciuria, nephrocalcinosis, and progressive renal failure. We sought to characterize the clinical manifestations and to identify the mu
- PMID 24428215
Japanese Journal
- HNK-1 sulfotransferase-dependent sulfation regulating laminin-binding glycans occurs in the post-phosphoryl moiety on α-dystroglycan.
- Glycobiology 23(9), 1066-1074, 2013-09
- NAID 120005474469
- Single Amino Acid Mutation around Flavin Cofactor Changes pH-Dependence of Basidiomycetes Class Ⅰ Cellobiose Dehydrogenase Activity
- Journal of applied glycoscience 60(2), 111-116, 2013-05-20
- NAID 10031159342
- Single amino acid residue in the A2 domain of major histocompatibility complex class I is involved in the efficiency of equine herpesvirus-1 entry.
- The Journal of biological chemistry 286(45), 39370-39378, 2011-11-11
- NAID 120005652751
Related Links
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★リンクテーブル★
| リンク元 | 「Thr residue」「スレオニン残基」「トレオニン残基」 |
| 関連記事 | 「residue」「threonine」 |
「Thr residue」
「スレオニン残基」
「トレオニン残基」
「residue」
- 関
- residual