Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition-Reference-Cited by-同舟云学术

Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition

Published:2021-04-20 Issue:17 Volume:60 Page:1347-1355
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Mateos Borja¹^ORCID,Holzinger Julian¹^ORCID,Conrad-Billroth Clara¹,Platzer Gerald¹^ORCID,Żerko Szymon²^ORCID,Sealey-Cardona Marco³,Anrather Dorothea⁴,Koźmiński Wiktor²^ORCID,Konrat Robert¹

Affiliation:

1. Department of Structural and Computational Biology, University of Vienna, Max Perutz Labs, Vienna BioCenter Campus 5, 1030 Vienna, Austria

2. Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, 02093 Warsaw, Poland

3. CALYXHA Biotechnologies GmbH, Karl-Farkas-Gasse 22, 1030 Vienna, Austria

4. Mass Spectrometry Facility, Max Perutz Laboratories, Vienna BioCenter Campus 5, Dr. Bohr Gasse 3, 1030 Vienna, Austria

Funder

Austrian Science Fund

Narodowe Centrum Nauki

Christian Doppler Forschungsgesellschaft

Bundesministerium f?r Digitalisierung und Wirtschaftsstandort

?sterreichische Nationalstiftung f?r Forschung, Technologie und Entwicklung

Christian Doppler Laboratory for High-Content Structural Biology and Biotechnology

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00050

Reference69 articles.

1. The importance of intrinsic disorder for protein phosphorylation

2. Structural Impact of Tau Phosphorylation at Threonine 231

3. Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation

4. Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain

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