About: Matthew B. Renfrow

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researcher

Attributes	Values
rdf:type	Item
description	ikertzailea (eu) researcher (en) 연구원 (ko) 研究者 (ja) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) 研究者 (zh) հետազոտող (hy)
rdfs:label	Matthew B. Renfrow (en) Matthew B. Renfrow (es) Matthew B. Renfrow (nl) Matthew B. Renfrow (sl) Matthew B. Renfrow (ast)
skos:prefLabel	Matthew B. Renfrow (en) Matthew B. Renfrow (es) Matthew B. Renfrow (nl) Matthew B. Renfrow (sl) Matthew B. Renfrow (ast)
name	Matthew B. Renfrow (en) Matthew B. Renfrow (es) Matthew B. Renfrow (nl) Matthew B. Renfrow (sl) Matthew B. Renfrow (ast)
Scopus author ID	wds:Q55080353-4EFD29AE-AF1A-49B7-B2CB-D0B9B4B18626
Scopus author ID	8852822600
given name	wds:Q55080353-96501BDC-E7C1-4928-A357-BFEE94404FF5
given name	Matthew
instance of	wds:Q55080353-604EECB3-03D3-48EF-B796-FE9E21472601
instance of	Homo sapiens
skos:altLabel	Matthew Renfrow (en)
occupation	wds:Q55080353-6B773EAC-88D2-4FBD-B4DC-4DEA87E0A557
employer	wds:Q55080353-A19D296F-A049-49C4-91DF-EDD3341E0DC9 wds:Q55080353-B45121FB-F149-475C-924E-53C8E36D624F
educated at	wds:Q55080353-B9EF6589-2F31-420D-B31A-E9C41A10F944 wds:Q55080353-CE44E7AC-C383-447E-A7B2-C72EC368703B
occupation	researcher
employer	University of Alabama at Birmingham National High Magnetic Field Laboratory
educated at	Western Kentucky University University of Georgia
ORCID iD	wds:Q55080353-11C8553D-48FE-40DB-AD46-78318323F594
ORCID iD	https://orcid.org/0000-0002-4193-7305
ORCID iD	0000-0002-4193-7305
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q55080353
is author of	Determination of aberrant O-glycosylation in the IgA1 hinge region by electron capture dissociation fourier transform-ion cyclotron resonance mass spectrometry. The RNA polymerase-associated factor 1 complex (Paf1C) directly increases the elongation rate of RNA polymerase I and is required for efficient regulation of rRNA synthesis. Structure, Energetics, and Dynamics of Binding Coactivator Peptide to the Human Retinoid X Receptor α Ligand Binding Domain Complex with 9- cis -Retinoic Acid Inactivation of human liver bile acid CoA:amino acid N-acyltransferase by the electrophilic lipid, 4-hydroxynonenal. SNO-hemoglobin is not essential for red blood cell-dependent hypoxic vasodilation Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition. Naturally occurring structural isomers in serum IgA1 o-glycosylation General N-and O-Linked Glycosylation of Lipoproteins in Mycoplasmas and Role of Exogenous Oligosaccharide O-linked protein glycosylation in Mycoplasma Biomarker discovery by CE-MS enables sequence analysis via MS/MS with platform-independent separation Atrial natriuretic peptide inhibits transforming growth factor beta-induced Smad signaling and myofibroblast transformation in mouse cardiac fibroblasts Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy Clustered O-glycans of IgA1: defining macro- and microheterogeneity by use of electron capture/transfer dissociation. Production of N-acetylgalactosaminyl-transferase 2 (GalNAc-T2) fused with secretory signal Igκ in insect cells Pathogenesis of immunoglobulin A nephropathy. Biomarkers in IgA nephropathy: relationship to pathogenetic hits. Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: implications for IgA nephropathy. Drosophila Orc6 facilitates GTPase activity and filament formation of the septin complex. Comparison of methods for profiling O-glycosylation: Human Proteome Organisation Human Disease Glycomics/Proteome Initiative multi-institutional study of IgA1 Tissue localization and solubilities of αA-crystallin and its numerous C-terminal truncation products in pre- and postcataractous ICR/f rat lenses active site modifications of the brain isoform of creatine kinase by 4-hydroxy-2-nonenal correlate with reduced enzyme activity: mapping of modified sites by Fourier transform-ion cyclotron resonance mass spectrometry Role of aberrant glycosylation of IgA1 molecules in the pathogenesis of IgA nephropathy Analysis of IgA1 N-glycosylation and its contribution to FcalphaRI binding Regulation of histone H2A and H2B deubiquitination and Xenopus development by USP12 and USP46. Ubp-M serine 552 phosphorylation by cyclin-dependent kinase 1 regulates cell cycle progression. Self-poisoning of Mycobacterium tuberculosis by interrupting siderophore recycling Training in metabolomics research. I. Designing the experiment, collecting and extracting samples and generating metabolomics data. Training in metabolomics research. II. Processing and statistical analysis of metabolomics data, metabolite identification, pathway analysis, applications of metabolomics and its future The Origin and Activities of IgA1-Containing Immune Complexes in IgA Nephropathy Transcription factor B contacts promoter DNA near the transcription start site of the archaeal transcription initiation complex Defining the Communication between Agonist and Coactivator Binding in the Retinoid X Receptor Ligand Binding Domain Somatic Mutations Modulate Autoantibodies against Galactose-Deficient IgA1 in IgA Nephropathy. Glycosylation in health and disease. Pyrazolopyrimidinones, a novel class of copper-dependent bactericidal antibiotics against multi-drug resistant S. aureus Serum galactose-deficient-IgA1 and IgG autoantibodies correlate in patients with IgA nephropathy. Glycosylation of viral surface proteins probed by mass spectrometry Probing conserved helical modules of portal complexes by mass spectrometry-based hydrogen/deuterium exchange. Phosphorylation of Pnut at the Early Steps of Drosophila Embryo Development Affects Association of the Septin Complex with Membrane and Is Important for Viability The Serum Very-Low-Density Lipoprotein Serves as a Restriction Factor against Hepatitis C Virus Infection. Efficient, ultra-high-affinity chromatography in a one-step purification of complex proteins. Aberrant Glycosylation of the IgA1 Molecule in IgA Nephropathy Human neutrophil peptide-1 inhibits thrombus formation under arterial flow via its terminal free cysteine thiols Role of remodeling and spacing factor 1 in histone H2A ubiquitination-mediated gene silencing. Training in metabolomics research. I. Designing the experiment, collecting and extracting samples and generating metabolomics data Defining HIV-1 Envelope N-glycan Microdomains Through Site-specific Heterogeneity Profiles N-acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy Rac1 modification by an electrophilic 15-deoxy Δ(12,14)-prostaglandin J2 analog. What insights can proteomics give us into IgA nephropathy (Berger's disease)? IgA1 hinge-region clustered glycan fidelity is established early during semi-ordered glycosylation by GalNAc-T2 Analysis of O-glycoforms of the IgA1 hinge region by sequential deglycosylation
is author of	wds:Q28551086-E6A295AD-641C-4E86-BB0B-A73B5027907F wds:Q28539595-E76A7A73-5E71-4A06-A86B-3B1158DB03E2

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