Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

Daniel J. Chin; Gregorio Gil; David W. Russell; Laura Liscum; Kenneth L. Luskey; Sandip K. Basu; Hiroto Okayama; Paul Berg; Joseph L. Goldstein; Michael S. Brown

doi:10.1038/308613a0

Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

Daniel J. Chin, Gregorio Gil, David W. Russell, Laura Liscum, Kenneth L. Luskey, Sandip K. Basu, Hiroto Okayama, Paul Berg, Joseph L. Goldstein, Michael S. Brown

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183 Scopus citations

Abstract

The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or Hydrophobie NH₂-terminal signal sequence.

Original language	English (US)
Pages (from-to)	613-617
Number of pages	5
Journal	Nature
Volume	308
Issue number	5960
DOIs	https://doi.org/10.1038/308613a0
State	Published - 1984

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title = "Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum",

abstract = "The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or Hydrophobie NH2-terminal signal sequence.",

author = "Chin, {Daniel J.} and Gregorio Gil and Russell, {David W.} and Laura Liscum and Luskey, {Kenneth L.} and Basu, {Sandip K.} and Hiroto Okayama and Paul Berg and Goldstein, {Joseph L.} and Brown, {Michael S.}",

year = "1984",

doi = "10.1038/308613a0",

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T1 - Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

AU - Chin, Daniel J.

AU - Gil, Gregorio

AU - Russell, David W.

AU - Liscum, Laura

AU - Luskey, Kenneth L.

AU - Basu, Sandip K.

AU - Okayama, Hiroto

AU - Berg, Paul

AU - Goldstein, Joseph L.

AU - Brown, Michael S.

PY - 1984

Y1 - 1984

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AB - The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or Hydrophobie NH2-terminal signal sequence.

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JO - Nature

JF - Nature

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ER -

Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

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