Structure and function of heme proteins regulated by diverse post-translational modifications-Reference-Cited by-同舟云学术

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Structure and function of heme proteins regulated by diverse post-translational modifications

Published:2018-03 Issue: Volume:641 Page:1-30
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Lin Ying-Wu

Funder

National Science Foundation of China

Hunan Provincial Natural Science Foundation for Distinguished Young Scholars

Scientific Research Fund of Hunan Provincial Education Department

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference295 articles.

1. Metalloenzymes, Structural Motifs, and Inorganic Models

2. Design of functional metalloproteins

3. The H93G myoglobin cavity mutant as a versatile scaffold for modeling heme iron coordination structures in protein active sites and their characterization with magnetic circular dichroism spectroscopy

4. Olefin Cyclopropanation via Carbene Transfer Catalyzed by Engineered Cytochrome P450 Enzymes

5. CO, NO and O2 as vibrational probes of heme protein interactions

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2. Elucidating the role of phytocompounds from Brassica oleracea var. italic (Broccoli) on hyperthyroidism: an in-silico approach;In Silico Pharmacology;2024-01-04

3. Design and engineering of an artificial disulfide bond in human cytochrome c to regulate the protein structure and function;Molecular Systems Design & Engineering;2024

4. Regulating the Heme Active Site by Covalent Modifications: Two Case Studies of Myoglobin;ChemBioChem;2023-12-12

5. Protective effect of thymoquinone on glycation of human myoglobin induced by d-ribose;International Journal of Biological Macromolecules;2023-12

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