PubMed:11099377 JSONTXT

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":129,"end":134},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T2","span":{"begin":221,"end":225},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T3","span":{"begin":535,"end":539},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T4","span":{"begin":1017,"end":1021},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T5","span":{"begin":1145,"end":1149},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T6","span":{"begin":1375,"end":1379},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T7","span":{"begin":1413,"end":1418},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T8","span":{"begin":1463,"end":1467},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T9","span":{"begin":1473,"end":1478},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T10","span":{"begin":1608,"end":1612},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T11","span":{"begin":1617,"end":1622},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T12","span":{"begin":1669,"end":1673},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T13","span":{"begin":1678,"end":1683},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T14","span":{"begin":1826,"end":1830},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T15","span":{"begin":1835,"end":1840},"obj":"https://acgg.asia/db/ggdb/info/gg170"}],"text":"Molecular cloning and expression of human UDP-d-Xylose:proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II.\nHuman UDP-d-xylose:proteoglycan core protein beta-d-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading frame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94% identity to the corresponding human enzyme."}

{"project":"PubMed_ArguminSci","denotations":[{"id":"T1","span":{"begin":136,"end":386},"obj":"DRI_Background"},{"id":"T2","span":{"begin":387,"end":616},"obj":"DRI_Approach"},{"id":"T3","span":{"begin":617,"end":824},"obj":"DRI_Background"},{"id":"T4","span":{"begin":825,"end":1006},"obj":"DRI_Background"},{"id":"T5","span":{"begin":1007,"end":1208},"obj":"DRI_Background"},{"id":"T6","span":{"begin":1209,"end":1380},"obj":"DRI_Background"},{"id":"T7","span":{"begin":1381,"end":1468},"obj":"DRI_Background"},{"id":"T8","span":{"begin":1469,"end":1588},"obj":"DRI_Background"},{"id":"T9","span":{"begin":1589,"end":1793},"obj":"DRI_Outcome"},{"id":"T10","span":{"begin":1794,"end":1862},"obj":"DRI_Background"},{"id":"T11","span":{"begin":1863,"end":1980},"obj":"DRI_Background"}],"text":"Molecular cloning and expression of human UDP-d-Xylose:proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II.\nHuman UDP-d-xylose:proteoglycan core protein beta-d-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading frame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94% identity to the corresponding human enzyme."}

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":129,"end":134},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T2","span":{"begin":221,"end":225},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T3","span":{"begin":535,"end":539},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T4","span":{"begin":1017,"end":1021},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T5","span":{"begin":1145,"end":1149},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T6","span":{"begin":1375,"end":1379},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T7","span":{"begin":1413,"end":1418},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T8","span":{"begin":1463,"end":1467},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T9","span":{"begin":1473,"end":1478},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T10","span":{"begin":1608,"end":1612},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T11","span":{"begin":1617,"end":1622},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T12","span":{"begin":1669,"end":1673},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T13","span":{"begin":1678,"end":1683},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"T14","span":{"begin":1826,"end":1830},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"T15","span":{"begin":1835,"end":1840},"obj":"https://acgg.asia/db/ggdb/info/gg170"}],"text":"Molecular cloning and expression of human UDP-d-Xylose:proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II.\nHuman UDP-d-xylose:proteoglycan core protein beta-d-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading frame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94% identity to the corresponding human enzyme."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":129,"end":134},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":221,"end":225},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":535,"end":539},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":1017,"end":1021},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":1145,"end":1149},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":1375,"end":1379},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":1413,"end":1418},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":1463,"end":1467},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":1473,"end":1478},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":1608,"end":1612},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":1617,"end":1622},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":1669,"end":1673},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":1678,"end":1683},"obj":"https://acgg.asia/db/ggdb/info/gg170"},{"id":"PD-GlycoGenes20190927-B_T14","span":{"begin":1826,"end":1830},"obj":"https://acgg.asia/db/ggdb/info/gg169"},{"id":"PD-GlycoGenes20190927-B_T15","span":{"begin":1835,"end":1840},"obj":"https://acgg.asia/db/ggdb/info/gg170"}],"text":"Molecular cloning and expression of human UDP-d-Xylose:proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II.\nHuman UDP-d-xylose:proteoglycan core protein beta-d-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading frame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94% identity to the corresponding human enzyme."}