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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

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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

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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

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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

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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

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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

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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

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[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

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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

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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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