Optimization of Protein Thermostability and Exploitation of Recognition Behavior to Engineer Altered Protein-DNA Recognition-Reference-Cited by-同舟云学术

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Optimization of Protein Thermostability and Exploitation of Recognition Behavior to Engineer Altered Protein-DNA Recognition

Published:2020-07 Issue:7 Volume:28 Page:760-775.e8
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Lambert Abigail R.,Hallinan Jazmine P.,Werther Rachel,Głów Dawid,Stoddard Barry L.

Funder

Mobilność Plus IV

Ministry of Science and Higher Education of Poland

NIH

Bluebird Bio, Inc.

Fred Hutchinson Cancer Research Center

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference41 articles.

1. The Rosetta all-atom energy function for macromolecular modeling and design;Alford;J. Chem. Theor. Comput.,2017

2. Mutational effects on stability are largely conserved during protein evolution;Ashenberg;Proc. Natl. Acad. Sci. U S A,2013

3. Computational reprogramming of homing endonuclease specificity at multiple adjacent base pairs;Ashworth;Nucleic Acids Res.,2010

4. Flow cytometric assays for interrogating LAGLIDADG homing endonuclease DNA-binding and cleavage properties;Baxter;Methods Mol. Biol.,2013

5. Engineering and flow-cytometric analysis of chimeric LAGLIDADG homing endonucleases from homologous I-OnuI-family enzymes;Baxter;Methods Mol. Biol.,2014

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2. Sequence-Directed Covalent Protein-RNA Linkages in a Single Step Using Engineered HUH-Tags;2024-08-13

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4. Opportunities and challenges in design and optimization of protein function;Nature Reviews Molecular Cell Biology;2024-04-02

5. Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design;Biochemistry;2022-03-04

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