Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Catherine L. Drennan"'
Publikováno v:
Biochemistry. 61:2797-2805
Ni-Fe-S-dependent carbon monoxide dehydrogenases (CODHs) are enzymes that interconvert CO and CO
Structural and Biochemical Investigations of the [4Fe-4S] Cluster-Containing Fumarate Hydratase from
Publikováno v:
Biochemistry
Class I fumarate hydratases (FHs) are central metabolic enzymes that use a [4Fe-4S] cluster to catalyze the reversible conversion of fumarate to S-malate. The parasite Leishmania major, which is responsible for leishmaniasis, expresses two class I FH
Autor:
Emily M. Zygiel, Elizabeth M. Nolan, Catherine L. Drennan, Toshiki G. Nakashige, Sarah E. J. Bowman
Publikováno v:
Biochemistry. 57:4155-4164
Calprotectin (CP, S100A8/S100A9 oligomer, MRP-8/MRP-14 oligomer) is a host-defense protein that sequesters nutrient transition metals from microbes. Each S100A8/S100A9 heterodimer contains four EF-hand domains and two transition-metal-binding sites.
Autor:
Samuel Thompson, Haoran Li, Julia E. Page, Catherine L. Drennan, Edward J. Brignole, Nozomi Ando, Francisco J. Asturias, JoAnne Stubbe, Martin I. McLaughlin
Publikováno v:
Biochemistry
Ribonucleotide reductases (RNRs) are responsible for all de novo biosynthesis of DNA precursors in nature by catalyzing the conversion of ribonucleotides to deoxyribonucleotides. Because of its essential role in cell division, human RNR is a target f
Autor:
Toshiki G, Nakashige, Sarah E J, Bowman, Emily M, Zygiel, Catherine L, Drennan, Elizabeth M, Nolan
Publikováno v:
Biochemistry. 57(28)
Calprotectin (CP, S100A8/S100A9 oligomer, MRP-8/MRP-14 oligomer) is a host-defense protein that sequesters nutrient transition metals from microbes. Each S100A8/S100A9 heterodimer contains four EF-hand domains and two transition-metal-binding sites.
Publikováno v:
Biochemistry
The soil actinomycete Kutzneria sp. 744 produces a class of highly decorated hexadepsipeptides, which represent a new chemical scaffold that has both antimicrobial and antifungal properties. These natural products, known as kutznerides, are created v
Autor:
Colin D. Douglas, Andrew M. Sydor, Catherine L. Drennan, Katherine S. Ryan, Kaitlyn E. Turo, Deborah B. Zamble, Marco Jost
Publikováno v:
Biochemistry
GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and met
Autor:
Jeremy W. Setser, Catherine L. Drennan, Gondichatnahalli M. Lingaraju, Leona D. Samson, C. Ainsley Davis
Publikováno v:
Biochemistry
To efficiently repair DNA, human alkyladenine DNA glycosylase (AAG) must search the million-fold excess of unmodified DNA bases to find a handful of DNA lesions. Such a search can be facilitated by the ability of glycosylases, like AAG, to interact w
Publikováno v:
Biochemistry
Exposure of Escherichia coli cells to small doses of DNA-methylating agents initiates a response that mitigates the mutagenic and cytotoxic effects of DNA methylation.1−3 This process, known as the adaptive response, involves the upregulation of fo
Publikováno v:
Biochemistry
Escherichia coli NikR regulates cellular nickel uptake by binding to the nik operon in the presence of nickel and blocking transcription of genes encoding the nickel uptake transporter. NikR has two binding affinities for the nik operon: a nanomolar