Results 131 to 140 of about 4,346 (168)

Molecular mechanism of naturally-encoded signaling-bias at the complement anaphylatoxin receptors

open access: yes
Tiwari D   +28 more
europepmc   +1 more source

Inhibition of C5AR1 impairs osteoclast mobilization and prevents bone loss

open access: yesMolecular Therapy, 2023
Age-related and chemotherapy-induced bone loss depends on cellular senescence and the cell secretory phenotype. However, the factors secreted in the senescent microenvironment that contribute to bone loss remain elusive. Here, we report a central role for the inflammatory alternative complement system in skeletal bone loss.
Francesc Ventura   +2 more
exaly   +3 more sources
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C5aR2 receptor: The genomic twin of the flamboyant C5aR1

Journal of Cellular Biochemistry, 2022
AbstractThe complement fragment C5a is one of the most potent proinflammatory glycoproteins liberated by the activation of the biochemical cascade of the complement system. C5a is established to interact with a set of genomically related transmembrane receptors, like C5aR1 (CD88, C5aR) and C5aR2 (GPR77, C5L2) with comparable affinity.
Aurosikha Das   +2 more
openaire   +2 more sources

Revealing the signaling of complement receptors C3aR and C5aR1 by anaphylatoxins

Nature Chemical Biology, 2023
The complement receptors C3aR and C5aR1, whose signaling is selectively activated by anaphylatoxins C3a and C5a, are important regulators of both innate and adaptive immune responses. Dysregulations of C3aR and C5aR1 signaling lead to multiple inflammatory disorders, including sepsis, asthma and acute respiratory distress syndrome.
Yue Wang   +12 more
openaire   +2 more sources

C5aR1

2018
C5aR1 is the lynchpin of communication between complement activation and the cellular immune response. It acts as a G-protein coupled receptor to attract and activate leucocytes in response to C5a. The genetic locus for C5aR1 consists of two exons separated by a large intron, a structure it shares with the other anaphylatoxin receptors.
Owen Hawksworth   +2 more
exaly   +5 more sources

Conformational variants of the ternary complex of C5a, C5aR1, and G-protein

open access: yesJournal of Biomolecular Structure and Dynamics
The complement component fragment 5a (C5a) binds and activates two complement receptors like C5aR1 and C5aR2, which play a significant role in orchestrating the proinflammatory function of C5a in tissues through the recruitment of heterotrimeric G-proteins and β-arrestins.
Soumendra Rana
exaly   +3 more sources

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