一种与大鼠蛋白质精氨酸N-甲基转移酶1（PRMT1）基因同源的新型人类基因HRMT1L1的鉴定与定位。 - Suppr

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超能文献

Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene.

作者信息

Katsanis N, Yaspo M L, Fisher E M

机构信息

Neurogenetics Unit, Imperial College School of Medicine at St. Mary's, Norfolk Place, London W2 1PG, UK.

出版信息

Mamm Genome. 1997 Jul;8(7):526-9. doi: 10.1007/s003359900491.

DOI:10.1007/s003359900491

PMID:9196002

Abstract

摘要

相似文献

Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene.一种与大鼠蛋白质精氨酸N-甲基转移酶1（PRMT1）基因同源的新型人类基因HRMT1L1的鉴定与定位。

Mamm Genome. 1997 Jul;8(7):526-9. doi: 10.1007/s003359900491.

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本文引用的文献

Generation and analysis of 280,000 human expressed sequence tags.280,000个人类表达序列标签的生成与分析。

Genome Res. 1996 Sep;6(9):807-28. doi: 10.1101/gr.6.9.807.

The gene encoding the p60 subunit of chromatin assembly factor I (CAF1P60) maps to human chromosome 21q22.2, a region associated with some of the major features of Down syndrome.编码染色质组装因子I（CAF1P60）p60亚基的基因定位于人类21号染色体q22.2区域，该区域与唐氏综合征的一些主要特征相关。

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Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant.人类和酵母HCP1基因的结构与功能保守性，该基因可抑制酿酒酵母ire15突变体的生长缺陷。

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A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins.一种新型甲基转移酶（Hmt1p）可修饰聚腺苷酸（poly(A)）+ RNA 结合蛋白。

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The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase.哺乳动物的即早基因TIS21蛋白和白血病相关蛋白BTG1与一种蛋白质精氨酸N-甲基转移酶相互作用。

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The I.M.A.G.E. Consortium: an integrated molecular analysis of genomes and their expression.I.M.A.G.E. 联盟：基因组及其表达的综合分子分析

Genomics. 1996 Apr 1;33(1):151-2. doi: 10.1006/geno.1996.0177.

Identification of a ten-amino acid proline-rich SH3 binding site.鉴定一个富含脯氨酸的十氨基酸SH3结合位点。

Science. 1993 Feb 19;259(5098):1157-61. doi: 10.1126/science.8438166.

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Genomics. 1994 Oct;23(3):700-3. doi: 10.1006/geno.1994.1561.

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