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Pesquisa : D12.125.068.555.478 [Categoria DeCS]
Referências encontradas : 695 [refinar]
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[PMID]:28006962
[Au] Autor:Gjaltema RA; Bank RA
[Ad] Endereço:a MATRIX Research Group, Department of Pathology and Medical Biology , University Medical Center Groningen, University of Groningen , Groningen , the Netherlands.
[Ti] Título:Molecular insights into prolyl and lysyl hydroxylation of fibrillar collagens in health and disease.
[So] Source:Crit Rev Biochem Mol Biol;52(1):74-95, 2017 Feb.
[Is] ISSN:1549-7798
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Collagen is a macromolecule that has versatile roles in physiology, ranging from structural support to mediating cell signaling. Formation of mature collagen fibrils out of procollagen α-chains requires a variety of enzymes and chaperones in a complex process spanning both intracellular and extracellular post-translational modifications. These processes include modifications of amino acids, folding of procollagen α-chains into a triple-helical configuration and subsequent stabilization, facilitation of transportation out of the cell, cleavage of propeptides, aggregation, cross-link formation, and finally the formation of mature fibrils. Disruption of any of the proteins involved in these biosynthesis steps potentially result in a variety of connective tissue diseases because of a destabilized extracellular matrix. In this review, we give a revised overview of the enzymes and chaperones currently known to be relevant to the conversion of lysine and proline into hydroxyproline and hydroxylysine, respectively, and the O-glycosylation of hydroxylysine and give insights into the consequences when these steps are disrupted.
[Mh] Termos MeSH primário: Colágenos Fibrilares/metabolismo
[Mh] Termos MeSH secundário: Animais
Artrogripose/metabolismo
Artrogripose/patologia
Doenças do Tecido Conjuntivo/metabolismo
Doenças do Tecido Conjuntivo/patologia
Síndrome de Ehlers-Danlos/metabolismo
Síndrome de Ehlers-Danlos/patologia
Colágenos Fibrilares/análise
Glicosilação
Seres Humanos
Hidroxilação
Hidroxilisina/análise
Hidroxilisina/metabolismo
Hidroxiprolina/análise
Hidroxiprolina/metabolismo
Lisina/análise
Lisina/metabolismo
Osteogênese Imperfeita/metabolismo
Osteogênese Imperfeita/patologia
Prolina/análise
Prolina/metabolismo
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Fibrillar Collagens); 2GQB349IUB (Hydroxylysine); 9DLQ4CIU6V (Proline); K3Z4F929H6 (Lysine); RMB44WO89X (Hydroxyproline)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161224
[St] Status:MEDLINE
[do] DOI:10.1080/10409238.2016.1269716


  2 / 695 MEDLINE  
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[PMID]:27379471
[Au] Autor:Behringer M; Montag JC; Kilian Y; Heaton P; Mester J
[Ad] Endereço:a Institute of Training Science and Sport Informatics , German Sport University Cologne , Cologne , Germany.
[Ti] Título:Polyamines, myosin heavy chains, and collagen specific amino acids after a repeated bout of eccentric exercise.
[So] Source:Res Sports Med;24(3):287-97, 2016 Jul-Sep.
[Is] ISSN:1543-8635
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We investigated alternatives to commonly used biomarkers of exercise-induced tissue damage. Over 5 days following two bouts of 100 drop-to-vertical jumps (inter-bout rest period of 3 weeks), myosin heavy chain 1, hydroxylysine (HYL), hydroxyproline (HYP), spermine (SPM) and spermine synthase (SMS) were measured in the serum of 10 participants. HYL significantly increased from 5.92 ± 1.49 ng/mL to 6.48 ± 1.47 ng/mL at 24 h. A similar trend was observed for bout 2, but without reaching significance. SPM significantly increased only after bout 1 from 0.96 ± 0.19 ng/mL at pretest to a peak level of 1.12 ± 0.26 ng/mL at 24 h, while B2 increments remained non-significant. Myosin heavy chain 1, HYP and SMS values remained below the detection limit of the applied enzyme-linked immunosorbent assay (ELISA) kit. Though HYL and SM increased after the intervention, both markers showed a large standard deviation (SD) combined with small increments. Therefore, none of the investigated biomarkers provides a meaningful alternative to commonly used damage markers.
[Mh] Termos MeSH primário: Exercício/fisiologia
Músculo Esquelético/patologia
Neutrófilos
[Mh] Termos MeSH secundário: Adulto
Biomarcadores/sangue
Seres Humanos
Hidroxilisina/sangue
Hidroxiprolina/sangue
Contagem de Leucócitos
Masculino
Mialgia/sangue
Mialgia/etiologia
Cadeias Pesadas de Miosina/sangue
Espermina/sangue
Espermina Sintase/sangue
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 2FZ7Y3VOQX (Spermine); 2GQB349IUB (Hydroxylysine); EC 2.5.1.22 (Spermine Synthase); EC 3.6.4.1 (Myosin Heavy Chains); RMB44WO89X (Hydroxyproline)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170330
[Lr] Data última revisão:
170330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160706
[St] Status:MEDLINE
[do] DOI:10.1080/15438627.2016.1202830


  3 / 695 MEDLINE  
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[PMID]:26797224
[Au] Autor:Raspanti M; Caravà E; Sgambato A; Natalello A; Russo L; Cipolla L
[Ad] Endereço:Department of Surgical & Morphological Sciences, Insubria University, Via Monte Generoso 71, 21100 Varese, Italy. Electronic address: mario.raspanti@uninsubria.it.
[Ti] Título:The collaggrecan: Synthesis and visualization of an artificial proteoglycan.
[So] Source:Int J Biol Macromol;86:65-70, 2016 May.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:An artificial aggrecan-like proteoglycan has been designed and synthesized in vitro. At variance with natural proteoglycans, whose glycosaminoglycan chains are always O-linked via a tetrasaccharide bridge to the serine residues of a specific protein core, the present structure consists of chondroitin-6-sulfate chains directly bound to the lysine and hydroxylysine residues of a collagen molecule backbone. The resulting macromolecule has been characterized by histochemistry, atomic force microscopy and FTIR. The number of variables involved (e.g., length and type of the collagen backbone, glycosaminoglycan species, sulfation type and pattern, molecular weight, number and length of side chains, etc.) makes possible to conceive an almost endless variety of artificial proteoglycans, each precisely tailored to a specific functional role. In addition to their use as biomaterials, glycated collagens interact with cells in complex ways and a previous study has already shown the ability of a glycated collagen to redirect fibroblastoma cells from proliferation to differentiation. The research is still underway.
[Mh] Termos MeSH primário: Materiais Biomiméticos/química
Materiais Biomiméticos/síntese química
Colágeno/química
Proteoglicanas/química
[Mh] Termos MeSH secundário: Animais
Bovinos
Técnicas de Química Sintética
Sulfatos de Condroitina/química
Hidroxilisina/química
Membranas Artificiais
Peso Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membranes, Artificial); 0 (Proteoglycans); 2GQB349IUB (Hydroxylysine); 9007-28-7 (Chondroitin Sulfates); 9007-34-5 (Collagen)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160123
[St] Status:MEDLINE


  4 / 695 MEDLINE  
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[PMID]:26661679
[Au] Autor:Li S; Lu J; Li J; Chen X; Yao X; Xi L
[Ad] Endereço:College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000, China.
[Ti] Título:HydPred: a novel method for the identification of protein hydroxylation sites that reveals new insights into human inherited disease.
[So] Source:Mol Biosyst;12(2):490-8, 2016 Feb.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The disruption of protein hydroxylation is highly associated with several serious diseases and consequently the identification of protein hydroxylation sites has attracted significant attention recently. Here, we report the development of an improved method, called HydPred, to identify protein hydroxylation sites (hydroxyproline and hydroxylysine) based on the synthetic minority over-sampling technique (SMOTE), the random forest (RF) algorithm and four blocks of newly composed features that are derived from the protein primary sequence. The HydPred method achieved the best prediction performance reported until now with Matthew's correlation coefficient values of 0.770 and 0.857 for hydroxyproline and hydroxylysine, respectively, according to jack-knife cross-validation. This represents an improvement of 8% for hydroxyproline and 19% for hydroxylysine compared to the best results of available predictors. The prediction performance of HydPred for the external validation of hydroxyproline and hydroxylysine was also improved compared with other published methods. We subsequently applied HydPred to study the association of disruption of hydroxylation sites with human inherited disease. The analyses suggested that the loss of hydroxylation sites is more likely to cause disease instead of the gain of hydroxylation sites and 52 different human inherited diseases were found to be highly associated with the loss of hydroxylation sites. Therefore, HydPred represents a new strategy to discover the molecular basis of pathogenesis associated with abnormal hydroxylation. HydPred is now available online as a user-friendly web server at http://lishuyan.lzu.edu.cn/hydpred/.
[Mh] Termos MeSH primário: Doenças Genéticas Inatas/metabolismo
Processamento de Proteína Pós-Traducional
Interface Usuário-Computador
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Doenças Genéticas Inatas/genética
Seres Humanos
Hidroxilação
Hidroxilisina/metabolismo
Hidroxiprolina/metabolismo
Curva ROC
Análise de Sequência de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
2GQB349IUB (Hydroxylysine); RMB44WO89X (Hydroxyproline)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1039/c5mb00681c


  5 / 695 MEDLINE  
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[PMID]:26651858
[Au] Autor:Xie Q; Moore B; Beardsley RL
[Ti] Título:Discovery and characterization of hydroxylysine in recombinant monoclonal antibodies.
[So] Source:MAbs;8(2):371-8, 2016.
[Is] ISSN:1942-0870
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tryptic peptide mapping analysis of a Chinese hamster ovary (CHO)-expressed, recombinant IgG1 monoclonal antibody revealed a previously unreported +16 Da modification. Through a combination of MS(n) experiments, and preparation and analysis of known synthetic peptides, the possibility of a sequence variant (Ala to Ser) was ruled out and the presence of hydroxylysine was confirmed. Post-translational hydroxylation of lysine was found in a consensus sequence (XKG) known to be the site of modification in other proteins such as collagen, and was therefore presumed to result from the activity of the CHO homolog of the lysyl hydroxylase complex. Although this consensus sequence was present in several locations in the antibody sequence, only a single site on the heavy-chain Fab was found to be modified.
[Mh] Termos MeSH primário: Anticorpos Monoclonais Humanizados/química
Hidroxilisina/química
Imunoglobulina G/química
[Mh] Termos MeSH secundário: Animais
Células CHO
Cricetinae
Cricetulus
Proteínas Recombinantes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Humanized); 0 (Immunoglobulin G); 0 (Recombinant Proteins); 2GQB349IUB (Hydroxylysine)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1080/19420862.2015.1122148


  6 / 695 MEDLINE  
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[PMID]:26565680
[Au] Autor:Zhang Y; Yu CY; Song E; Li SC; Mechref Y; Tang H; Liu X
[Ad] Endereço:Department of Computer Science, City University of Hong Kong , Kowloon, Hong Kong.
[Ti] Título:Identification of Glycopeptides with Multiple Hydroxylysine O-Glycosylation Sites by Tandem Mass Spectrometry.
[So] Source:J Proteome Res;14(12):5099-108, 2015 Dec 04.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycosylation is one of the most common post-translational modifications in proteins, existing in ~50% of mammalian proteins. Several research groups have demonstrated that mass spectrometry is an efficient technique for glycopeptide identification; however, this problem is still challenging because of the enormous diversity of glycan structures and the microheterogeneity of glycans. In addition, a glycopeptide may contain multiple glycosylation sites, making the problem complex. Current software tools often fail to identify glycopeptides with multiple glycosylation sites, and hence we present GlycoMID, a graph-based spectral alignment algorithm that can identify glycopeptides with multiple hydroxylysine O-glycosylation sites by tandem mass spectra. GlycoMID was tested on mass spectrometry data sets of the bovine collagen α-(II) chain protein, and experimental results showed that it identified more glycopeptide-spectrum matches than other existing tools, including many glycopeptides with two glycosylation sites.
[Mh] Termos MeSH primário: Algoritmos
Glicopeptídeos/análise
Glicopeptídeos/metabolismo
Hidroxilisina/metabolismo
Espectrometria de Massas em Tandem/métodos
[Mh] Termos MeSH secundário: Animais
Cartilagem/química
Bovinos
Colágeno Tipo II/metabolismo
Glicosilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type II); 0 (Glycopeptides); 2GQB349IUB (Hydroxylysine)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151205
[Lr] Data última revisão:
151205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151114
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.5b00299


  7 / 695 MEDLINE  
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[PMID]:26036128
[Au] Autor:Zaitseva OV; Shandrenko SG; Veliky MM
[Ti] Título:Biochemical markers of bone collagen type I metabolism.
[So] Source:Ukr Biochem J;87(1):21-32, 2015 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:This review focuses on the analysis of diagnostic value of the major bone remodeling markers, in particular synthesis and degradation markers of collagen type I. These include carboxy- and aminoterminal telopeptide, carboxy- and aminoterminal propeptide of procollagen type I, hydroxyproline, hydroxylysine, pyridinoline and deoxypyridinoline. Their measurement allows evaluating the structural and functional conditions and also the rate of metabolic processes in the bone tissue. The advantages and disadvantages of determination of these markers in the condition of different bone diseases were examined. It is shown that determination of bone collagen type I metabolism markers is the most informative for assessment of bone resorption, formation and turnover.
[Mh] Termos MeSH primário: Reabsorção Óssea/sangue
Reabsorção Óssea/urina
Osso e Ossos/metabolismo
Colágeno Tipo I/metabolismo
Pró-Colágeno/metabolismo
[Mh] Termos MeSH secundário: Fosfatase Ácida/metabolismo
Fosfatase Alcalina/metabolismo
Aminoácidos/sangue
Aminoácidos/urina
Animais
Biomarcadores/sangue
Biomarcadores/urina
Densidade Óssea
Reabsorção Óssea/patologia
Osso e Ossos/patologia
Seres Humanos
Hidroxilisina/sangue
Hidroxilisina/urina
Hidroxiprolina/sangue
Hidroxiprolina/urina
Osteocalcina/metabolismo
Fragmentos de Peptídeos/sangue
Fragmentos de Peptídeos/urina
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Amino Acids); 0 (Biomarkers); 0 (Collagen Type I); 0 (Peptide Fragments); 0 (Procollagen); 104982-03-8 (Osteocalcin); 2GQB349IUB (Hydroxylysine); 63800-01-1 (pyridinoline); 90032-33-0 (deoxypyridinoline); EC 3.1.3.1 (Alkaline Phosphatase); EC 3.1.3.2 (Acid Phosphatase); RMB44WO89X (Hydroxyproline)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150604
[St] Status:MEDLINE


  8 / 695 MEDLINE  
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Texto completo
[PMID]:25948757
[Au] Autor:Hill RC; Wither MJ; Nemkov T; Barrett A; D'Alessandro A; Dzieciatkowska M; Hansen KC
[Ad] Endereço:From the ‡Department of Biochemistry and Molecular Genetics, University of Colorado Denver, Aurora, Colorado 80045, USA.
[Ti] Título:Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen.
[So] Source:Mol Cell Proteomics;14(7):1946-58, 2015 Jul.
[Is] ISSN:1535-9484
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bone samples from several vertebrates were collected from the Ziegler Reservoir fossil site, in Snowmass Village, Colorado, and processed for proteomics analysis. The specimens come from Pleistocene megafauna Bison latifrons, dating back ∼ 120,000 years. Proteomics analysis using a simplified sample preparation procedure and tandem mass spectrometry (MS/MS) was applied to obtain protein identifications. Several bioinformatics resources were used to obtain peptide identifications based on sequence homology to extant species with annotated genomes. With the exception of soil sample controls, all samples resulted in confident peptide identifications that mapped to type I collagen. In addition, we analyzed a specimen from the extinct B. latifrons that yielded peptide identifications mapping to over 33 bovine proteins. Our analysis resulted in extensive fibrillar collagen sequence coverage, including the identification of posttranslational modifications. Hydroxylysine glucosylgalactosylation, a modification thought to be involved in collagen fiber formation and bone mineralization, was identified for the first time in an ancient protein dataset. Meta-analysis of data from other studies indicates that this modification may be common in well-preserved prehistoric samples. Additional peptide sequences from extracellular matrix (ECM) and non-ECM proteins have also been identified for the first time in ancient tissue samples. These data provide a framework for analyzing ancient protein signatures in well-preserved fossil specimens, while also contributing novel insights into the molecular basis of organic matter preservation. As such, this analysis has unearthed common posttranslational modifications of collagen that may assist in its preservation over time. The data are available via ProteomeXchange with identifier PXD001827.
[Mh] Termos MeSH primário: Colágeno/metabolismo
Extinção Biológica
Hidroxilisina/metabolismo
Espectrometria de Massas em Tandem/métodos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Asparagina/metabolismo
Bison
Colágeno/química
Glutamina/metabolismo
Glicosilação
Dados de Sequência Molecular
Crânio/anatomia & histologia
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0RH81L854J (Glutamine); 2GQB349IUB (Hydroxylysine); 7006-34-0 (Asparagine); 9007-34-5 (Collagen)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170412
[Lr] Data última revisão:
170412
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150508
[St] Status:MEDLINE
[do] DOI:10.1074/mcp.M114.047787


  9 / 695 MEDLINE  
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[PMID]:25757225
[Au] Autor:Hayashi G; Sakamoto R; Okamoto A
[Ad] Endereço:Department of Chemistry and Biotechnology, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656 (Japan).
[Ti] Título:2-Oxazoline formation for selective chemical labeling of 5-hydroxylysine.
[So] Source:Chem Asian J;10(5):1138-41, 2015 May.
[Is] ISSN:1861-471X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Hydroxylation of lysine, one of posttranslational modifications of proteins, generates 5-hydroxylysine (Koh) and plays a crucial role in regulating protein functions in cellular activity. We have developed a chemical labeling method of Koh. The 1,2-aminoalcohol moiety of Koh in synthetic peptide sequences was trapped by an alkyne-containing benzimidate to form a 2-oxazoline ring. An additional ammonia treatment process removed the undesirable amidine residue formed between benzimidate and lysine. During the ammonia treatment, the oxazoline residue formed at Koh mainly remained intact, and the ring opening to the amide form was observed for only part of oxazoline, indicating that the chemical labeling is amino acid selective. Azide-substituted biotin or fluorescent dye was attached to the peptide through Huisgen cycloaddition at Koh and converted into an alkyne-labeled oxazoline form. The Koh-labeling assay could provide a platform to enhance proteomic research of lysine hydroxylation.
[Mh] Termos MeSH primário: Hidroxilisina/análogos & derivados
Oxazóis/síntese química
Coloração e Rotulagem/métodos
[Mh] Termos MeSH secundário: Hidroxilisina/análise
Hidroxilisina/química
Estrutura Molecular
Oxazóis/química
Proteômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oxazoles); 2GQB349IUB (Hydroxylysine)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150311
[St] Status:MEDLINE
[do] DOI:10.1002/asia.201500172


  10 / 695 MEDLINE  
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[PMID]:25113599
[Au] Autor:Guo L; Liu T; Chen K; Song T; Wang PG; Zhao W
[Ad] Endereço:State Key Laboratory of Medicinal Chemical Biology and College of Pharmacy, Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin 300071, PR China. wzhao@nankai.edu.cn pwang@nankai.edu.cn.
[Ti] Título:Facile synthesis of 5-hydroxy-L-lysine from D-galactose as a chiral-precursor.
[So] Source:Org Biomol Chem;12(37):7310-7, 2014 Oct 07.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A concise synthesis of (2S,5R) and (2S,5S)-5-hydroxy-lysine was achieved by utilizing D-galactose as a chiral-precursor with stereo retention. This synthetic strategy showcased the potential of utilizing carbohydrates as starting materials to prepare amino acids. Using the diazido intermediate, the derived ß-D-galactopyranosyl and α-D-glucopyranosyl-(1→2)-ß-D-galactosyl moieties were synthesized.
[Mh] Termos MeSH primário: Galactose/química
Hidroxilisina/síntese química
[Mh] Termos MeSH secundário: Hidroxilisina/química
Conformação Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
2GQB349IUB (Hydroxylysine); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:140828
[Lr] Data última revisão:
140828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140813
[St] Status:MEDLINE
[do] DOI:10.1039/c4ob01220h



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