Samuel G Gattis
Overview
Explore the profile of Samuel G Gattis including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
11
Citations
346
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Dollins D, Bai W, Fridy P, Otto J, Neubauer J, Gattis S, et al.
Proc Natl Acad Sci U S A
. 2020 Apr;
117(17):9356-9364.
PMID: 32303658
Inositol diphosphates (PP-IPs), also known as inositol pyrophosphates, are high-energy cellular signaling codes involved in nutrient and regulatory responses. We report that the evolutionarily conserved gene product, Vip1, possesses autonomous...
2.
Gattis S, Chung H, Trent M, Raetz C
J Biol Chem
. 2013 Feb;
288(13):9216-25.
PMID: 23413030
Lipopolysaccharide (LPS; endotoxin) is an essential component of the outer monolayer of nearly all Gram-negative bacteria. LPS is composed of a hydrophobic anchor, known as lipid A, an inner core...
3.
Cole K, Gattis S, Angell H, Fierke C, Christianson D
Biochemistry
. 2010 Dec;
50(2):258-65.
PMID: 21171638
The first committed step of lipid A biosynthesis is catalyzed by UDP-(3-O-((R)-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase, a metal-dependent deacetylase also known as LpxC. Because lipid A is essential for bacterial viability, the inhibition...
4.
Gattis S, Hernick M, Fierke C
J Biol Chem
. 2010 Aug;
285(44):33788-96.
PMID: 20709752
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate in Gram-negative bacteria. This second, and committed, step in lipid A biosynthesis is a target for antibiotic...
5.
Dowling D, Gattis S, Fierke C, Christianson D
Biochemistry
. 2010 Jun;
49(24):5048-56.
PMID: 20545365
The metal-dependent histone deacetylases (HDACs) adopt an alpha/beta protein fold first identified in rat liver arginase. Despite insignificant overall amino acid sequence identity, these enzymes share a strictly conserved metal...
6.
Hernick M, Gattis S, Penner-Hahn J, Fierke C
Biochemistry
. 2010 Feb;
49(10):2246-55.
PMID: 20136146
The metal-dependent deacetylase UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase (LpxC) catalyzes the first committed step in lipid A biosynthesis, the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate. Consequently, LpxC is a target for...
7.
Rider L, Ottosen M, Gattis S, Palfey B
J Biol Chem
. 2009 Jan;
284(16):10324-33.
PMID: 19139092
Dihydrouridine synthases (DUSs) are flavin-dependent enzymes that catalyze site-specific reduction of uracils in tRNAs. The mechanism of DUS 2 from Saccharomyces cerevisiae was studied. Previously published turnover rates for this...
8.
Dowling D, Gantt S, Gattis S, Fierke C, Christianson D
Biochemistry
. 2008 Dec;
47(51):13554-63.
PMID: 19053282
Metal-dependent histone deacetylases (HDACs) require Zn(2+) or Fe(2+) to regulate the acetylation of lysine residues in histones and other proteins in eukaryotic cells. Isozyme HDAC8 is perhaps the archetypical member...
9.
Wolfe A, Thymark M, Gattis S, Fagan R, Hu Y, Johansson E, et al.
Biochemistry
. 2007 Apr;
46(19):5741-53.
PMID: 17444658
Dihydroorotate dehydrogenases (DHODs) catalyze the oxidation of dihydroorotate to orotate in the only redox reaction in pyrimidine biosynthesis. The pyrimidine binding sites are very similar in all structurally characterized DHODs,...
10.
Gantt S, Gattis S, Fierke C
Biochemistry
. 2006 May;
45(19):6170-8.
PMID: 16681389
Histone deacetylases play a key role in regulating transcription and other cellular processes by catalyzing the hydrolysis of epsilon-acetyl-lysine residues. For this reason, inhibitors of histone deacetylases are potential targets...