Structural basis of the GM2 gangliosidosis B variant
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H. Doi | H. Sakuraba | A. Tanaka | H. Ninomiya | K. Ohno | F. Matsuzawa | S. Aikawa | Y. Sugimoto | Hoàng Thi Ngoc Lan
[1] Timm Maier,et al. The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease. , 2003, Journal of molecular biology.
[2] M. James,et al. Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. , 2003, Journal of molecular biology.
[3] H. Doi,et al. Molecular and structural studies of the GM2 gangliosidosis 0 variant , 2002, Journal of Human Genetics.
[4] S. Withers,et al. Crystallographic Evidence for Substrate-assisted Catalysis in a Bacterial β-Hexosaminidase* , 2001, The Journal of Biological Chemistry.
[5] Zbigniew Dauter,et al. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay–Sachs disease , 1996, Nature Structural Biology.
[6] G. Isshiki,et al. Molecular genetics of Tay-Sachs disease in Japan , 1994, Journal of Inherited Metabolic Disease.
[7] M. Natowicz,et al. A new Tay-Sachs disease B1 allele in exon 7 in two compound heterozygotes each with a second novel mutation. , 1992, Human molecular genetics.
[8] J. Clarke,et al. Sequence of DNA flanking the exons of the HEXA gene, and identification of mutations in Tay-Sachs disease. , 1991, American journal of human genetics.
[9] M. Ribeiro,et al. GM2-gangliosidosis B1 variant: analysis of beta-hexosaminidase alpha gene mutations in 11 patients from a defined region in Portugal. , 1991, American journal of human genetics.
[10] J. Chelly,et al. Seven novel Tay-Sachs mutations detected by chemical mismatch cleavage of PCR-amplified cDNA fragments. , 1991, Genomics.
[11] E. Nanba,et al. Expression of the beta-hexosaminidase alpha subunit gene with the four-base insertion of infantile Jewish Tay-Sachs disease. , 1991, The Journal of biological chemistry.
[12] B. Paw,et al. A third mutation at the CpG dinucleotide of codon 504 and a silent mutation at codon 506 of the HEX A gene. , 1991, American journal of human genetics.
[13] R. Boustany,et al. Genetic cause of a juvenile form of tay‐sachs disease in a lebanese child , 1991, Annals of neurology.
[14] B. Paw,et al. Juvenile GM2 gangliosidosis caused by substitution of histidine for arginine at position 499 or 504 of the alpha-subunit of beta-hexosaminidase. , 1990, The Journal of biological chemistry.
[15] A. Brown,et al. GM2-gangliosidosis B1 variant: analysis of beta-hexosaminidase alpha gene abnormalities in seven patients. , 1990, American journal of human genetics.
[16] D. Mahuran,et al. Introduction of the alpha subunit mutation associated with the B1 variant of Tay-Sachs disease into the beta subunit produces a beta-hexosaminidase B without catalytic activity. , 1989, The Journal of biological chemistry.
[17] R. Myerowitz,et al. The major defect in Ashkenazi Jews with Tay-Sachs disease is an insertion in the gene for the alpha-chain of beta-hexosaminidase. , 1988, The Journal of biological chemistry.
[18] B. Paw,et al. Normal transcription of the beta-hexosaminidase alpha-chain gene in the Ashkenazi Tay-Sachs mutation. , 1988, The Journal of biological chemistry.
[19] K. Ohno,et al. Mutation in GM2‐Gangliosidosis B1 Variant , 1988, Journal of neurochemistry.
[20] T L Blundell,et al. Knowledge based modelling of homologous proteins, Part II: Rules for the conformations of substituted sidechains. , 1987, Protein engineering.
[21] T. A. Jones,et al. Using known substructures in protein model building and crystallography. , 1986, The EMBO journal.
[22] K. Sandhoff,et al. Variant of GM2‐gangliosidosis with hexosaminidase A having a severely changed substrate specificity. , 1983, The EMBO journal.
[23] W. Kabsch. A discussion of the solution for the best rotation to relate two sets of vectors , 1978 .
[24] W. Kabsch. A solution for the best rotation to relate two sets of vectors , 1976 .
[25] A. Tanaka,et al. A New Point Mutation in the 0-Hexosaminidase a Subunit Gene Responsible for Infantile Tay-Sachs Disease in a Non-Jewish Caucasian Patient (a Kpn Mutant) , 2006 .
[26] G. Isshiki,et al. Novel mutations, including the second most common in Japan, in the beta-hexosaminidase alpha subunit gene, and a simple screening of Japanese patients with Tay-Sachs disease. , 1999, Journal of human genetics.
[27] A. Kahn,et al. Ten novel mutations in the HEXA gene in non-Jewish Tay-Sachs patients. , 1993, Human molecular genetics.
[28] G. Isshiki,et al. The major mutation among Japanese patients with infantile Tay-Sachs disease: a G-to-T transversion at the acceptor site of intron 5 of the beta-hexosaminidase alpha gene. , 1993, Biochemical and biophysical research communications.
[29] G. Thomas,et al. Six novel deleterious and three neutral mutations in the gene encoding the alpha-subunit of hexosaminidase A in non-Jewish individuals. , 1992, American journal of human genetics.
[30] S. Wodak,et al. Modelling the polypeptide backbone with 'spare parts' from known protein structures. , 1989, Protein engineering.
[31] K. Ohno,et al. GM2-gangliosidosis B1 variant: a wide geographic and ethnic distribution of the specific beta-hexosaminidase alpha chain mutation originally identified in a Puerto Rican patient. , 1988, Biochemical and biophysical research communications.
[32] K. Suzuki. Enzymatic diagnosis of sphingolipidoses. , 1987, Methods in enzymology.
[33] H. Berman,et al. Electronic Reprint Biological Crystallography the Protein Data Bank Biological Crystallography the Protein Data Bank , 2022 .