Heat treatment of thioredoxin fusions increases the purity of α‐helical transmembrane protein constructs-Reference-Cited by-同舟云学术

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Heat treatment of thioredoxin fusions increases the purity of α‐helical transmembrane protein constructs

Published:2021-07-06 Issue:9 Volume:30 Page:1974-1982
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Schenkel Mathias¹,Treff Antoine¹,Deber Charles M.²,Krainer Georg¹³^ORCID,Schlierf Michael¹^ORCID

Affiliation:

1. B CUBE – Center for Molecular Bioengineering TU Dresden Dresden Germany

2. Division of Molecular Medicine, Research Institute Hospital for Sick Children Toronto Ontario Canada

3. Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry University of Cambridge Cambridge UK

Funder

Boehringer Ingelheim Stiftung

Canadian Institutes of Health Research

Cystic Fibrosis Canada

European Social Fund

H2020 Marie Skłodowska-Curie Actions

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4150

Reference36 articles.

1. An Introduction to Membrane Proteins

2. Introduction to membrane proteins;Chiu ML;Curr Protoc Protein Sci,2012

3. How many drug targets are there?

4. Misfolding of membrane proteins in health and disease: the lady or the tiger?

5. Drugging Membrane Protein Interactions

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1. Maltodextrin-modified hyperoxic graphene oxide as potential matrix for one-step purification and immobilization of MBP-tagged proteins;Separation and Purification Technology;2025-01

2. Heating-mediated purification of active FGF21 and structure-based design of its variant with enhanced potency;Scientific Reports;2023-01-18

3. Impact of cholesterol and Lumacaftor on the folding of CFTR helical hairpins;Biochimica et Biophysica Acta (BBA) - Biomembranes;2023-01

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