HDX‐MS reveals orthosteric and allosteric changes in apolipoprotein‐D structural dynamics upon binding of progesterone-Reference-Cited by-同舟云学术

HDX‐MS reveals orthosteric and allosteric changes in apolipoprotein‐D structural dynamics upon binding of progesterone

Published:2018-12-20 Issue:2 Volume:28 Page:365-374
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Kielkopf Claudia S.¹²³,Ghosh Madhubrata⁴,Anand Ganesh S.⁴,Brown Simon H.J.¹²³^ORCID

Affiliation:

1. Illawarra Health and Medical Research InstituteUniversity of Wollongong Wollongong New South Wales Australia

2. Molecular HorizonsUniversity of Wollongong Wollongong New South Wales Australia

3. School of Biological SciencesUniversity of Wollongong Wollongong New South Wales Australia

4. Department of Biological SciencesNational University of Singapore Singapore

Funder

University of Wollongong

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3534

Reference36 articles.

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4. Site‐specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion;Pa S;Protein Sci,1995

5. Selective reduction of hydroperoxyeicosatetraenoic acids to their hydroxy derivatives by apolipoprotein D: implications for lipid antioxidant activity and Alzheimer's disease

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