A structural perspective on the PP-loop ATP pyrophosphatase family-Reference-Cited by-同舟云学术

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A structural perspective on the PP-loop ATP pyrophosphatase family

Published:2018-10-03 Issue:6 Volume:53 Page:607-622
ISSN:1040-9238
Container-title:Critical Reviews in Biochemistry and Molecular Biology
language:en
Short-container-title:Critical Reviews in Biochemistry and Molecular Biology

Author:

Fellner Matthias¹^ORCID,Hausinger Robert P.¹²^ORCID,Hu Jian¹³^ORCID

Affiliation:

1. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA;

2. Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI, USA;

3. Department of Chemistry, Michigan State University, East Lansing, MI, USA

Funder

National Science Foundation

University of Otago Health Sciences Postdoctoral Fellowship

Publisher

Informa UK Limited

Subject

Molecular Biology,Biochemistry

Link

https://www.tandfonline.com/doi/pdf/10.1080/10409238.2018.1516728

Reference80 articles.

1. Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA world

2. Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster

3. Active site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation

4. The Reported Human NADsyn2 Is Ammonia-dependent NAD Synthetase from a Pseudomonad

5. A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast

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3. Structural Characterization of an N-Acetyl Sugar Amidotransferase Involved in the Lipopolysaccharide Biosynthesis in Bacteria;International Journal of Molecular Sciences;2023-10-23

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