Effects of Mutations Involving Cysteine Residues Distal to the S281HCC Motif at the C-Terminus on the Functional Characteristics of a Truncated Ectodomain-Only Thyrotropin Receptor Anchored on Glycosylphosphatidyl-Inositol-Reference-Cited by-同舟云学术

Effects of Mutations Involving Cysteine Residues Distal to the S281HCC Motif at the C-Terminus on the Functional Characteristics of a Truncated Ectodomain-Only Thyrotropin Receptor Anchored on Glycosylphosphatidyl-Inositol

Published:2008-12 Issue:12 Volume:18 Page:1313-1319
ISSN:1050-7256
Container-title:Thyroid
language:en
Short-container-title:Thyroid

Author:

Ho Su-Chin¹²,Goh Sui-Sin³,Li Sun⁴,Khoo Daphne Hsu-Chin²,Paterson Malcolm¹

Affiliation:

1. SingHealth Research, Singapore Health Service, Singapore, Republic of Singapore.

2. Department of Endocrinology, Singapore General Hospital, Singapore, Republic of Singapore.

3. Department of Pathology, Singapore General Hospital, Singapore, Republic of Singapore.

4. Clinical Research, Singapore General Hospital, Singapore, Republic of Singapore.

Publisher

Mary Ann Liebert Inc

Subject

Endocrinology,Endocrinology, Diabetes and Metabolism

Link

https://www.liebertpub.com/doi/pdf/10.1089/thy.2008.0240

Reference30 articles.

1. Disulfide Bonds and Protein Folding

2. Oxidative Folding of Proteins

3. Substantial increase of protein stability by multiple disulphide bonds

4. Protein Disulfide Bond Formation in Prokaryotes

5. Disulfide bonds as switches for protein function

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