Role of amino acid residues at the interface of alpha52asparginyl-N-glycosyl chain of human choriogonadotropin (Q38322716)

2 September 2017

title

Role of amino acid residues at the interface of alpha52asparginyl-N-glycosyl chain of human choriogonadotropin (English)

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2 September 2017

Shao K

1

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2 September 2017

Balasubramanian SV

series ordinal

2

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2 September 2017

Bahl OP

series ordinal

3

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2 September 2017

publication date

1 April 1999

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Molecular and Cellular Endocrinology

2 September 2017

published in

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2 September 2017

volume

150

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2 September 2017

issue

1-2

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2 September 2017

page(s)

47-56

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

2 September 2017

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Reversible folding of human chorionic gonadotropin at acid pH or upon recombination of the alpha and beta subunits

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The biological role of the carboxyl-terminal extension of human chorionic gonadotropin [corrected] beta-subunit

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The carboxyl-terminal region is a determinant for the intracellular behavior of the chorionic gonadotropin beta subunit: effects on the processing of the Asn-linked oligosaccharides

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Effect of modification of the beta-hairpin and long loops simultaneously in both alpha- and beta-subunits on the function of human choriogonadotropin: part II.

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Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein

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Replacement of the invariant tyrosine in the CAGY region of the human chorionic gonadotropin β subunit

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7 January 2021

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Identifiers

DOI

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2 September 2017

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