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副粘病毒猴病毒5的血凝素神经氨酸酶蛋白:mRNA的核苷酸序列预测有一个N端膜锚定序列。

Hemagglutinin-neuraminidase protein of the paramyxovirus simian virus 5: nucleotide sequence of the mRNA predicts an N-terminal membrane anchor.

作者信息

Hiebert S W, Paterson R G, Lamb R A

出版信息

J Virol. 1985 Apr;54(1):1-6. doi: 10.1128/JVI.54.1.1-6.1985.

Abstract

The nucleotide sequence of a cloned cDNA copy of the mRNA coding for the hemagglutinin-neuraminidase of the paramyxovirus SV5 was determined. There was a single large open reading frame on the mRNA which encoded a protein of 565 amino acids with a molecular weight of 62,134. The deduced amino acid sequence indicated that the only major hydrophobic region in the protein sufficiently long to anchor the protein in the membrane is located near the N terminus (amino acids 18 to 36). It is suggested that, like the influenza virus neuraminidase, hemagglutinin-neuraminidase of paramyxoviruses is oriented with its N terminus inserted into the membrane.

摘要

测定了副粘病毒SV5编码血凝素神经氨酸酶的mRNA的克隆cDNA拷贝的核苷酸序列。该mRNA上有一个单一的大开放阅读框,编码一个由565个氨基酸组成、分子量为62134的蛋白质。推导的氨基酸序列表明,该蛋白质中唯一足够长以将其锚定在膜中的主要疏水区域位于N端附近(氨基酸18至36)。有人提出,与流感病毒神经氨酸酶一样,副粘病毒的血凝素神经氨酸酶也是以其N端插入膜中的方式定向的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6779/254752/6cd7e66d52a7/jvirol00121-0014-a.jpg

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