about
Expansion of protein farnesyltransferase specificity using "tunable" active site interactions: development of bioengineered prenylation pathways.Identification of a novel class of farnesylation targets by structure-based modeling of binding specificity.Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities.Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substratesSynthetic Triterpenoid Inhibition of Human Ghrelin O-Acyltransferase: The Involvement of a Functionally Required Cysteine Provides Mechanistic Insight into Ghrelin Acylation.Simultaneous Site-Specific Dual Protein Labeling Using Protein Prenyltransferases.Context-dependent substrate recognition by protein farnesyltransferase.Structure-activity analysis of human ghrelin O-acyltransferase reveals chemical determinants of ghrelin selectivity and acyl group recognition.A new class of ghrelin O-acyltransferase inhibitors incorporating triazole-linked lipid mimetic groups.The 2'-hydroxyl group of the guanosine nucleophile donates a functionally important hydrogen bond in the tetrahymena ribozyme reaction.Improved synthesis of 2'-amino-2'-deoxyguanosine and its phosphoramidite.Efficient farnesylation of an extended C-terminal C(x)3X sequence motif expands the scope of the prenylated proteome.Simultaneous Analysis of a Non-Lipidated Protein and Its Lipidated Counterpart: Enabling Quantitative Investigation of Protein Lipidation's Impact on Cellular Regulation.The octanoylated energy regulating hormone ghrelin: An expanded view of ghrelin's biological interactions and avenues for controlling ghrelin signaling.Ghrelin Octanoylation Is Completely Stabilized in Biological Samples by Alkyl Fluorophosphonates.Getting a handle on protein prenylation.Targeted reengineering of protein geranylgeranyltransferase type I selectivity functionally implicates active-site residues in protein-substrate recognition.Quantitative determination of cellular farnesyltransferase activity: towards defining the minimum substrate reactivity for biologically relevant protein farnesylation.Using selective withdrawal to coat microparticlesAn atomic mutation cycle for exploring RNA's 2'-hydroxyl groupSynthesis of frame-shifted farnesyl diphosphate analogsA fluorescent peptide substrate facilitates investigation of ghrelin recognition and acylation by ghrelin O-acyltransferaseFunctional group and stereochemical requirements for substrate binding by ghrelin O-acyltransferase revealed by unnatural amino acid incorporationProtein Farnesyltransferase Catalyzes Unanticipated Farnesylation and Geranylgeranylation of Shortened Target SequencesGhrelin Signaling: GOAT and GHS-R1a Take a LEAP in ComplexityGhrelin octanoylation by ghrelin O-acyltransferase: Unique protein biochemistry underlying metabolic signalingProtein Isoprenylation in Yeast Targets COOH-Terminal Sequences Not Adhering to the CaaX ConsensusBiochemical Assays for Ghrelin Acylation and Inhibition of Ghrelin O-AcyltransferaseThe ghrelin O-acyltransferase structure reveals a catalytic channel for transmembrane hormone acylationAn overview of ghrelin O-acyltransferase inhibitors: a literature and patent review for 2010-2019
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
James L Hougland
@nl
James L Hougland
@sl
James L. Hougland
@en
James L. Hougland
@es
type
label
James L Hougland
@nl
James L Hougland
@sl
James L. Hougland
@en
James L. Hougland
@es
prefLabel
James L Hougland
@nl
James L Hougland
@sl
James L. Hougland
@en
James L. Hougland
@es
P106
P1153
7801478003
P21
P31
P496
0000-0003-0444-1017