Isabelle Ronsse

Rega Institute for Medical Research — Belgium

Medicine · Health Sciences

18h-index1.3kcitations32works0.02yr avg
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Research Topics

Chemokine receptors and signaling(14), Cell Adhesion Molecules Research(13), Immune Response and Inflammation(9), Protease and Inhibitor Mechanisms(6), Proteoglycans and glycosaminoglycans research(5)

Publications32 total

Proteoform Analysis of Matrix Metalloproteinase-9/Gelatinase B and Discovery of Its Citrullination in Rheumatoid Arthritis Synovial Fluids
Frontiers in Immunology·2021· 14 citedOpen Access
Anti‐inflammatory effects of the <scp>GAG</scp>‐binding <scp>CXCL</scp>9(74‐103) peptide in dinitrofluorobenzene‐induced contact hypersensitivity in mice
Clinical & Experimental Allergy·2018· 10 cited
Monocytes from patients with Primary Ciliary Dyskinesia show enhanced inflammatory properties and produce higher levels of pro-inflammatory cytokines
Scientific Reports·2017· 17 citedOpen Access
Relative distribution and biological characterization of CXCL4L1 isoforms in platelets from healthy donors
Biochemical Pharmacology·2017· 4 citedOpen Access
Recombinant Parvoviruses Armed to Deliver CXCL4L1 and CXCL10 Are Impaired in Their Antiangiogenic and Antitumoral Effects in a Kaposi Sarcoma Tumor Model Due To the Chemokines' Interference with the Virus Cycle
Human Gene Therapy·2017· 11 cited
The COOH-terminal GAG binding CXCL9(74-103) peptide inhibits CXCL8-induced neutrophil extravasation and monosodium urate crystal-induced gout in mice
2016
The Positively Charged CXCL9(74-103) Peptide Competes for GAG Binding with Inflammatory Chemokines and Inhibits Chemokine-Induced Neutrophil Extravasation and MSU Crystal-Induced Gout in Mice
2016
The positively charged glycosaminoglycan-binding CXCL9-derived peptide, CXCL9(74-103), inhibits CXCL8-induced neutrophil extravasation and monosodium urate crystal- induced gout in mice
2015
The Positively Charged COOH-terminal Glycosaminoglycan-binding CXCL9(74–103) Peptide Inhibits CXCL8-induced Neutrophil Extravasation and Monosodium Urate Crystal-induced Gout in Mice
Journal of Biological Chemistry·2015· 62 citedOpen Access
Intradermal air pouch leukocytosis as an in vivo test for nanoparticles
International Journal of Nanomedicine·2013· 28 citedOpen Access
Citrullination of TNF-α by peptidylarginine deiminases reduces its capacity to stimulate the production of inflammatory chemokines
Cytokine·2012· 31 cited
Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation
PLoS ONE·2011· 32 citedOpen Access
Posttranslational Modification of the NH2-terminal Region of CXCL5 by Proteases or Peptidylarginine Deiminases (PAD) Differently Affects Its Biological Activity
Journal of Biological Chemistry·2010· 57 citedOpen Access
The COOH-Terminal Peptide of Platelet Factor-4 Variant (CXCL4L1/PF-4var47-70) Strongly Inhibits Angiogenesis and Suppresses B16 Melanoma Growth <i>In vivo</i>
Molecular Cancer Research·2010· 43 citedOpen Access
Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
The Journal of Cell Biology·2008· 6 cited
Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
The Journal of Experimental Medicine·2008· 175 citedOpen Access
Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation
Blood·2008· 134 cited
CD13/aminopeptidase N-processed I-TAC/CXCL11 has reduced CXCR3 and CXCR7 binding and signaling properties that result in impaired lymphocyte chemotaxis and reduced inhibition of endothelial cell migration
2008
Proteolytic processing of CXCL11 by CD13/aminopeptidase N impairs CXCR3 and CXCR7 binding and signaling and reduces lymphocyte and endothelial cell migration
Blood·2007· 132 citedOpen Access
TLR ligands and cytokines induce CXCR3 ligands in endothelial cells: enhanced CXCL9 in autoimmune arthritis
Laboratory Investigation·2006· 112 citedOpen Access
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Frequent Co-authors

Jo Van Damme(23), Paul Proost(21), Ghislain Opdenakker(16), Anneleen Mortier(12), Sofie Struyf(12), Mieke Gouwy(10), Nele Berghmans(9), Tamara Loos(8), Evemie Schutyser(7), Rik Janssens(6), Willy Put(5), Vincent Vanheule(5), Pierre Fiten(5), Alfons Billiau(5), Chris Dillen(4), René Conings(4), Bernard Grillet(4), Inge Nelissen(4), Daiane Boff(4), Flávio A. Amaral(4)