Results 181 to 190 of about 10,590 (201)

Chemokine Receptors CXCR3 and CXCR7

, 2012
openaire   +1 more source

The role of macrophage and adipocyte mitochondrial dysfunction in the pathogenesis of obesity. [PDF]

Front Immunol
Wang M, Min M, Duan H, Mai J, Liu X.
europepmc   +1 more source

A cytokine receptor-targeting chimera toolbox for expanding extracellular targeted protein degradation. [PDF]

Proc Natl Acad Sci U S A
Kumru K, Yao Z, Holmes BB, Zhao F, Zhang Y, Ferrara E, Peters-Clarke TM, Leung KK, Wells JA.   +8 more
europepmc   +1 more source

CXCL12 no hatsugen wa shokudo henpei johigan no zoshoku o sokushinshi, yogo o akkasaseru [PDF]

Uchi, Yusuke, ウチ, ユウスケ, 内, 雄介   +2 more
core   +1 more source

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Resonating with the signaling bias of CXCR7

Molecular Cell, 2022
Kleist et al. combine NMR spectroscopy and residue contact network analysis to identify a potential allosteric network in CXCR7, a β-arrestin-biased chemokine receptor, which links the extracellular ligand-binding pocket and the intracellular transducer-coupling region through the receptor transmembrane core.
Parishmita, Sarma, Arun K, Shukla
openaire   +2 more sources

CXCR7, CXCR4 and CXCL12: An eccentric trio?

Journal of Neuroimmunology, 2008
CXCR7, formerly called RDC1 is a recently deorphanized G-protein coupled receptor which binds with high affinity the inflammatory and homing chemokines CXCL11/ITAC and CXCL12/SDF-1. Despite its phylogenetic relation and ligand binding properties CXCR7 does not mediate typical chemokine receptor responses such as leukocyte trafficking.
Marcus, Thelen, Sylvia, Thelen
openaire   +2 more sources

Shifting Signals with CXCR7

Science Signaling, 2011
CXCR7 heterodimerizes with CXCR4, leading to preferential activation of β-arrestin–mediated signaling pathways.
openaire   +1 more source

SDF‐1α induces differential trafficking of CXCR4‐CXCR7 involving cyclophilin A, CXCR7 ubiquitination and promotes platelet survival

The FASEB Journal, 2014
ABSTRACT Platelet‐derived SDF‐1α (CXCL12) mediates inflammatory and regenerative mechanisms. The present study characterizes the effect of SDF‐1α ligation in platelets. SDF‐1α (0–100 μM) dose and time dependently caused internalization of its receptor CXCR4 (28.9±1.6 vs . 16.
Chatterjee, Madhumita, Seizer, Peter, Borst, Oliver, Mack, Andreas F., Geisler, Tobias, Langer, Harald, May, Andreas E., Vogel, Sebastian, Lang, Florian, Gawaz, Meinrad Paul, Schönberger, Tanja   +10 more
openaire   +3 more sources