The FKBP-Type Domain of the Human Aryl Hydrocarbon Receptor-Interacting Protein Reveals an Unusual Hsp90 Interaction-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

The FKBP-Type Domain of the Human Aryl Hydrocarbon Receptor-Interacting Protein Reveals an Unusual Hsp90 Interaction

Published:2013-03-13 Issue:12 Volume:52 Page:2097-2107
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Linnert Miriam¹,Lin Yi-Jan²,Manns Annika¹,Haupt Katja¹,Paschke Anne-Katrin¹,Fischer Gunter¹,Weiwad Matthias¹,Lücke Christian¹

Affiliation:

1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany

2. Graduate Institute of Natural Products and Center of Excellence for Environmental Medicine, Kaohsiung Medical University, Kaohsiung 807, Taiwan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi301649m

Reference50 articles.

1. Ligand-dependent Interaction of the Aryl Hydrocarbon Receptor with a Novel Immunophilin Homolog in Vivo

2. Receptor accessory folding helper enzymes: the functional role of peptidyl prolylcis/transisomerases

3. Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes

4. 3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex

Cited by 38 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Familial isolated pituitary adenoma is independent of Ahr genotype in a novel mouse model of disease;Heliyon;2024-04

2. The aryl hydrocarbon receptor-interacting protein in cancer and immunity: Beyond a chaperone protein for the dioxin receptor;Journal of Biological Chemistry;2024-04

3. Cryo-EM structure of the agonist-bound Hsp90-XAP2-AHR cytosolic complex;Nature Communications;2022-11-16

4. The Role of Hsp90 in Retinal Proteostasis and Disease;Biomolecules;2022-07-12

5. Cryo-EM structure of the agonist-bound Hsp90-XAP2-AHR cytosolic complex;2022-05-17

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号京ICP备18003416号-3