A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I)-Reference-Cited by-同舟云学术

A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I)

Published:2020-11-02 Issue:44 Volume:59 Page:4238-4249
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Liu Xinyue¹,Garber Abigail²,Ryan Julia²,Deshpande Aditi³^ORCID,Ringe Dagmar¹³⁴,Pochapsky Thomas C.¹³⁴^ORCID

Affiliation:

1. Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454-9110, United States

2. Department of Biology, Brandeis University, 415 South Street, Waltham, Massachusetts 02454-9110, United States

3. Department of Biochemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454-9110, United States

4. Rosenstiel Institute for Basic Biomedical Research, Brandeis University, 415 South Street, Waltham, Massachusetts 02454-9110, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00724

Reference31 articles.

1. Human Acireductone Dioxygenase (HsARD), Cancer and Human Health: Black Hat, White Hat or Gray?

2. The Methionine Salvage Pathway in Klebsiella pneumoniae and Rat Liver

3. Mechanistic Studies of Two Dioxygenases in the Methionine Salvage Pathway of Klebsiella pneumoniae,

4. One Protein, Two Enzymes

5. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae

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