Maria Di Girolamo

ORCID: 0000-0002-9842-0446
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • PARP inhibition in cancer therapy
  • Toxin Mechanisms and Immunotoxins
  • Calcium signaling and nucleotide metabolism
  • Inflammatory Bowel Disease
  • Liver Disease Diagnosis and Treatment
  • Cellular transport and secretion
  • Microscopic Colitis
  • Ion channel regulation and function
  • Liver Diseases and Immunity
  • Protein Kinase Regulation and GTPase Signaling
  • Eosinophilic Esophagitis
  • Biosimilars and Bioanalytical Methods
  • Signaling Pathways in Disease
  • Distributed and Parallel Computing Systems
  • Erythrocyte Function and Pathophysiology
  • Thyroid Disorders and Treatments
  • Pancreatitis Pathology and Treatment
  • Service-Oriented Architecture and Web Services
  • Health Systems, Economic Evaluations, Quality of Life
  • Liver Disease and Transplantation
  • Electrostatic Discharge in Electronics
  • Organ Transplantation Techniques and Outcomes
  • Spondyloarthritis Studies and Treatments
  • Celiac Disease Research and Management
  • Autoimmune and Inflammatory Disorders

Azienda Unita' Sanitaria Locale Di Modena
2019-2023

University of Modena and Reggio Emilia
2016-2020

Mario Negri Sud Foundation
2005-2018

Shiga University of Medical Science
2016

Juntendo University
2016

Azienda Ospedaliero-Universitaria di Modena
2013-2015

Azienda Ospedaliera San Camillo-Forlanini
2014

Sapienza University of Rome
2014

University of Rome Tor Vergata
2013

Western General Hospital
2013

Journal Article Energy-Efficient Cloud Computing Get access Andreas Berl, Berl * 1Fakultät für Informatik und Mathematik, University of Passau, Innstr. 43, 94032 Germany *Corresponding author: berl@uni-passau.de Search for other works by this author on: Oxford Academic Google Scholar Erol Gelenbe, Gelenbe 2Electrical and Electronic Engineering Department, Imperial College London, South Kensington Campus, London SW7 2AZ, UK Marco Di Girolamo, Girolamo 3HP-European Innovation Centre, HP IIC...

10.1093/comjnl/bxp080 article EN The Computer Journal 2009-08-19

The chemokine CXC ligand 8 (CXCL8)/IL-8 and related agonists recruit activate polymorphonuclear cells by binding the receptor 1 (CXCR1) CXCR2. Here we characterize unique mode of action a small-molecule inhibitor (Repertaxin) CXCR1 Structural biochemical data are consistent with noncompetitive allosteric interaction between Repertaxin, which, locking in an inactive conformation, prevents signaling. Repertaxin is effective cell recruitment vivo protects organs against reperfusion injury....

10.1073/pnas.0402090101 article EN Proceedings of the National Academy of Sciences 2004-07-28

Liver fibrosis is critical for liver-related outcomes and mortality in chronic liver disease, irrespective of etiology, including nonalcoholic fatty disease (NAFLD). NAFLD has been viewed as an independent correlate cardiovascular risk. This review article briefly describes the cellular molecular pathomechanisms underlying hepatic fibrosis. We then address noninvasive assessment Finally, we discuss published evidence supporting biomarkers’ role assessing risk among patients with NAFLD. While...

10.20517/mtod.2022.23 article EN Metabolism and Target Organ Damage 2023-01-01

Mono-ADP-ribosylation is a reversible posttranslational modification that modulates the function of target proteins. The enzymes catalyze this reaction in mammalian cells are either bacterial pathogenic toxins or endogenous cellular ADP-ribosyltransferases. For latter, both and their targets have largely remained elusive, mainly due to lack specific techniques study reaction. recent discovery macro domain, protein module interacts selectively with ADP-ribose, prompted us investigate whether...

10.1073/pnas.0900066106 article EN Proceedings of the National Academy of Sciences 2009-02-26

Background Protein mono-ADP-ribosylation is a reversible post-translational modification that modulates the function of target proteins. The enzymes catalyze this reaction in mammalian cells are either bacterial pathogenic toxins or endogenous cellular ADP-ribosyltransferases. latter include members three different families proteins: well characterized arginine-specific ecto-enzymes ARTCs, two sirtuins and, more recently, novel poly(ADP-ribose) polymerase (PARP/ARTD) family have been...

10.1371/journal.pone.0037352 article EN cc-by PLoS ONE 2012-06-11

Abstract Non-alcoholic fatty liver disease (NAFLD) can be detected in up to 33.6% of inflammatory bowel (IBD) patients, often absence metabolic risk factors. Nevertheless, most previous studies on such issue were conducted within the IBD population only. The primary aim this study was compare clinical and features NAFLD patients with without (w/o IBD) identify specific phenotypes population. Among 223 78 younger compared 145 (w/o) IBD, less likely have altered enzymes, had lower mean body...

10.1038/s41419-017-0124-2 article EN cc-by Cell Death and Disease 2018-01-24

We report a prospective, nationwide cohort evaluating the safety and effectiveness of CT-P13.A structured database was used to record serious adverse events (SAEs), clinical remission/response, inflammatory biomarkers (CRP calprotectin), endoscopic findings.Eight hundred ten patients with bowel disease (IBD) (452 Crohn's [CD]) were enrolled. Four fifty-nine naïve anti-TNFα (group A), 196 had previous exposure B), remaining 155 switched CT-P13 C). All included in evaluation mean follow-up 345...

10.1093/ibd/izy264 article EN Inflammatory Bowel Diseases 2018-08-18

Brefeldin A (BFA) is a fungal metabolite that exerts profound and generally inhibitory actions on membrane transport. At least some of the BFA effects are due to inhibition GDP-GTP exchange ADP-ribosylation factor (ARF) catalyzed by protein(s). ARF activation likely be key event in association non-clathrin coat components, including itself, onto transport organelles. ARF, addition participating transport, known function as cofactor enzymatic activity cholera toxin, bacterial...

10.1073/pnas.91.3.1114 article EN Proceedings of the National Academy of Sciences 1994-02-01

Mono-ADP-ribosylation is a post-translational modification of cellular proteins that has been implicated in the regulation signal transduction, muscle cell differentiation, protein trafficking, and secretion. In several systems we have observed major substrate endogenous mono-ADP-ribosylation 36-kDa protein. This ADP-ribosylated was both recognized Western blotting experiments selectively immunoprecipitated by G β subunit-specific polyclonal antibody, indicating this subunit. The...

10.1074/jbc.275.13.9418 article EN cc-by Journal of Biological Chemistry 2000-03-01

Brefeldin A, a fungal metabolite that inhibits membrane transport, induces the mono(ADP-ribosyl)ation of two cytosolic proteins 38 and 50 kDa as judged by SDS/PAGE. The 38-kDa substrate has been previously identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH). We report 50-kDa BFA-induced ADP-ribosylated (BARS-50) native forms 170 130 kDa, determined gel filtration rat brain cytosol, indicating BARS-50 might exist multimeric complex. can bind GTP, indicated blot-overlay studies with...

10.1073/pnas.92.15.7065 article EN Proceedings of the National Academy of Sciences 1995-07-18

The mechanism of phospholipase C regulation by inhibitory receptors was analyzed both in intact and permeabilized rat thyroid cells (FRTL5). In this system, the muscarinic agonist carbachol inhibited C, as indicated decrease basal levels inositol 1,4,5-trisphosphate well reduced adrenergic stimulation phosphoinositol accumulation, which paralleled a fall cytosolic Ca2+ levels. This inhibition involved an M2 receptor because it abolished atropine but not M1 antagonist pirenzepine. Cells...

10.1073/pnas.87.12.4889 article EN Proceedings of the National Academy of Sciences 1990-06-01

Ctcf (CCCTC-binding factor) directly induces Parp [poly(ADP-ribose) polymerase] 1 activity and its PARylation [poly(ADPribosyl)ation] in the absence of DNA damage. Ctcf, turn, is a substrate for this post-synthetic modification as such it covalently non-covalently modified by PARs (ADP-ribose polymers). Moreover, able to protect certain regions bound from methylation. We recently reported that de novo methylation target sequences due overexpression Parg [poly(ADP-ribose)glycohydrolase] loss...

10.1042/bj20121429 article EN Biochemical Journal 2012-11-05

Brefeldin A, a toxin inhibitor of vesicular traffic, induces the selective mono-ADP-ribosylation two cytosolic proteins, glyceraldehyde-3-phosphate dehydrogenase and novel GTP-binding protein BARS-50. Here, we have used new quantitative assay for characterization this reaction development specific pharmacological inhibitors. Mono-ADP-ribosylation is activated by brefeldin A with an EC50 17.0 ± 3.1 μg/ml, but not biologically inactive analogs including stereoisomer. acts increasing theVmax...

10.1074/jbc.272.22.14200 article EN cc-by Journal of Biological Chemistry 1997-05-01

Post-translational modifications of cellular proteins by mono- or poly-ADP-ribosylation are associated with numerous processes. ADP-ribosylation reactions important in the nucleus, and mitochondrial activity, stress response signaling, intracellular trafficking, cell senescence apoptosis decisions. These reversible add ADP-ribose to target via specific enzymes form ADP-ribosylated protein; cleaveage this covalent bond is performed hydrolases. Deficiencies these enzymatic activities lead...

10.2174/138161213804581882 article EN Current Pharmaceutical Design 2012-12-20

We have recently demonstrated that the beta subunit of heterotrimeric G-proteins is endogenously mono-ADP-ribosylated in intact cells. The modified betagamma heterodimer loses its ability to inhibit calmodulin-stimulated type 1 adenylate cyclase and, remarkably, de-ADP-ribosylated by a cytosolic hydrolase completes an ADP-/de-ADP-ribosylation cycle potential physiological relevance. In present study, we show this ADP-ribosylation might indeed be general mechanism for termination signalling,...

10.1042/bj20020660 article EN Biochemical Journal 2002-10-25

Abstract The isoenzyme pattern of N-acetyl-beta-glucosaminidase (NAG) in serum and urine was studied two groups patients with diabetes mellitus 30 control subjects. Total NAG activity significantly (P less than 0.001) increased the 20 diabetics vascular complications, but insignificantly without complications. Ion-exchange chromatography demonstrated presence major isoenzymes NAG, A B. proportion always exceeded that B lower controls; reverse true for diabetics. may provide additional...

10.1093/clinchem/34.12.2430 article EN Clinical Chemistry 1988-12-01
Coming Soon ...