N
Nikolaus Heveker
Researcher at Université de Montréal
Publications - 64
Citations - 5072
Nikolaus Heveker is an academic researcher from Université de Montréal. The author has contributed to research in topics: Chemokine receptor & Receptor. The author has an hindex of 36, co-authored 64 publications receiving 4741 citations. Previous affiliations of Nikolaus Heveker include Centre Hospitalier Universitaire Sainte-Justine & Université de Sherbrooke.
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Identification of a chemokine receptor encoded by human cytomegalovirus as a cofactor for HIV-1 entry.
TL;DR: The human cytomegalovirus encodes a beta-chemokine receptor (US28) that is distantly related to the human chemokine receptors CCR5 and CXCR4, which also serve as cofactors for the entry into cells of human immunodeficiency virus-type 1 (HIV-1).
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AMD3100 Is a CXCR7 Ligand with Allosteric Agonist Properties
Irina Kalatskaya,Yamina A. Berchiche,Stéphanie Gravel,Brian Joseph Limberg,Jan S. Rosenbaum,Nikolaus Heveker +5 more
TL;DR: The data suggest that AMD3100 is an allosteric agonist of CXCR7, and calls for caution in the use of the compound as a tool to dissect CXCL12 effects on the respective receptors in vitro and in vivo.
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Bioluminescence resonance energy transfer reveals ligand-induced conformational changes in CXCR4 homo- and heterodimers
Yann Percherancier,Yamina A. Berchiche,Isabelle Slight,Rudolf Volkmer-Engert,Hirokazu Tamamura,Nobutaka Fujii,Michel Bouvier,Nikolaus Heveker +7 more
TL;DR: The formation of CXCR4 and CCR2 chemokine receptor dimers is investigated and it is found that both receptors exist as constitutive homo- and heterodimers and that ligands induce conformational changes within the pre-formed dimers without promoting receptor dimer formation or disassembly.
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Identification of Residues of CXCR4 Critical for Human Immunodeficiency Virus Coreceptor and Chemokine Receptor Activities
TL;DR: The identification of CXCR4 residues involved in the interaction with both SDF-1 and HIV-1 may account for the signaling activity of gp120 and has implications for the development of antiviral compounds.
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Monomeric and dimeric CXCL12 inhibit metastasis through distinct CXCR4 interactions and signaling pathways.
Luke J. Drury,Joshua J. Ziarek,Stéphanie Gravel,Christopher T. Veldkamp,Christopher T. Veldkamp,Tomonori Takekoshi,Samuel T Hwang,Nikolaus Heveker,Brian F. Volkman,Michael B. Dwinell +9 more
TL;DR: It is shown that administration of CXCL12 extended survival of tumor-bearing mice by potently limiting metastasis of colorectal carcinoma or murine melanoma and concluded that cellular migration is tightly regulated by selective CXCR4 signaling evoked by unique interactions with distinct ligand quaternary structures.