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Boston, MA and Irvine, CA — [March 18, 2026]  — Dr. GPCR, a nonprofit organization serving the global G protein-coupled receptor (GPCR) research community through education, curated scientific content, and community engagement, today announced a strategic media partnership with GeneTex, a multinational antibody manufacturer with long-standing expertise in reagent development and validation. Anti-GPCR antibody specificity has been a persistent challenge in the field — one with real consequences for data reproducibility. This partnership exists to bring that conversation into the open, and to invite GPCR researchers to be part of the solution. GeneTex is offering free antibody samples to the community — not as a promotion, but as a direct scientific challenge That challenge is well recognized: the specificity and reliability of anti-GPCR antibodies, and the downstream impact these limitations have on the reproducibility of GPCR-related data. Given the structural complexity and dynamic nature of GPCRs, generating antibodies that selectively and consistently recognize their intended targets remains a significant technical challenge. Concerns around antibody specificity are not merely theoretical. When antibodies fail to selectively recognize GPCR targets, the resulting data can be difficult to reproduce. These challenges have contributed to ongoing debate within the field regarding how antibody-based data should be interpreted and contextualized in GPCR research and GPCR drug discovery. This partnership seeks to bring those challenges into clearer scientific focus by placing GeneTex’s GPCR-focused antibody efforts within an open, community-wide conversation. The collaboration reflects a shared recognition that improving data reproducibility in GPCR biology requires continued attention to antibody specificity, validation strategies, and transparent discussion of limitations. GeneTex is developing a comprehensive portfolio of recombinant antibodies targeting human non-sensory and orphan GPCRs. These efforts are supported by characterization approaches that include knockout/knockdown testing, endogenous receptor detection, and comparative analyses. Through this partnership, GeneTex’s antibody portfolio is introduced to the GPCR community as part of a broader discussion about how antibody quality influences data reliability and reproducibility. Researchers working on GPCR targets are invited to request free samples through the Dr. GPCR partnership page, evaluate the antibodies in their own experimental systems, and share their findings — positive or negative. Community feedback is central to how this partnership is designed to work. “Challenges around anti-GPCR antibody specificity have real consequences for the reproducibility of GPCR data,” said Dr. Yamina Berchiche , Founder and CEO of Dr. GPCR. “As a nonprofit organization, our role is not to validate reagents, but to ensure that these issues are openly discussed and scientifically contextualized. This partnership reflects our commitment to advancing conversations that directly affect how GPCR research is conducted and interpreted.” “GPCRs present unique challenges for antibody development,” said Alexander Ball, Jr., M.D., Senior Scientist at GeneTex. “We see value in situating our antibody efforts within an open scientific dialogue focused on specificity, reliability, and the reproducibility of the data generated using these tools. Thorough validation and engagement with the GPCR researcher community are both essential for realizing our goal of producing trusted antibody reagents for GPCR biologists.” For the GPCR research community, the relevance of this partnership extends beyond individual reagents. Reproducible data are foundational to progress in GPCR biology, target validation, and translational research. When antibody specificity is uncertain, variability in experimental outcomes can propagate across studies, complicating interpretation and slowing progress. By explicitly acknowledging these challenges, the partnership aligns with broader efforts across the life sciences to improve data reproducibility by addressing limitations at the level of research tools. It reinforces the importance of transparency and community engagement in strengthening the experimental foundations that support GPCR research and GPCR drug discovery. Together, Dr. GPCR and GeneTex aim to support informed, critical dialogue around anti-GPCR antibody specificity and the reproducibility of GPCR data, contributing to a more robust and reliable foundation for the field. About Dr. GPCR Dr. GPCR is a nonprofit organization connecting the global GPCR community through training, curated scientific news, expert-led courses, and networking. Through educational programs, media initiatives, and a growing partner ecosystem, Dr. GPCR supports scientists and organizations advancing GPCR biology and GPCR-targeted drug discovery. About GeneTex GeneTex is a multinational antibody manufacturer founded in 1997, with research and manufacturing operations across the United States, Taiwan, and Europe. GeneTex develops antibodies and reagents supporting a broad range of biomedical research areas, with ongoing efforts focused on recombinant monoclonal anti-GPCR antibodies targeting human GPCRs using rigorous characterization approaches. To learn more about the Dr. GPCR–GeneTex partnership, visit: GeneTex Partnership Page

Discover how Revvity’s pHSense™ reagents enable real-time GPCR internalization detection A breakthrough GPCR internalization assay now featured in the Dr. Developed to address long-standing challenges in GPCR internalization assays , pHSense™ reagents  combine “The day we saw dose-dependent internalization in endogenous GLP1R cells—without microscopy—that was A GPCR Internalization Tool Designed for Real Research Needs Built on more than two decade A GPCR Internalization

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a wide range of mechanisms of action, including cAMP accumulation, β-arrestin recruitment, receptor internalization flux, and ligand binding, generating multidimensional datasets trusted by leading pharmaceutical and biotechnology

Upon agonist activation, the DOR-APEX2 complex is internalized and trafficked to the lysosome.

Classically, GPCR internalization has been considered to lead to receptor desensitization. However, many studies over the past decade have reported that internalized membrane receptors can trigger The "internalized activation" provides a completely new understanding for the receptor internalization Here, this review summarizes different PTMs in GPCR internalization and analyzes their significance in GPCR internalization dynamics, internalization routes, postinternalization fates, and related diseases

Actions Adher’n Rise and ERNEST plus DFG-funded CRC1423 and RU2372) have joined forces to organize an international We aim to connect renowned international experts of the field with early career ‘rising stars’.

GPCRs are present in a range of conformations, and the binding of a ligand, as well as interactions with Depending on the specific functional outcome measured (e.g. activation, interaction with accessory proteins , dimerization, phosphorylation, internalization, or desensitization), the same drug acting on the same

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"We are moving ahead with SLAS2022 as an in-person event with a hybrid component. We are closely monitoring any regulation changes from both Boston and Massachusetts with regard to in-person events. If there are any changes made that will impact our ability to hold the event in-person, we will notify the SLAS community as soon as possible. Please refer to our Safe Meeting guidelines for information about how you can participate in the event in-person. Don't miss the chance to present your innovative research at this year's conference. Poster abstracts for in-person and virtual presentations will be accepted through Monday, January 24." Register here

September 2022 Interacting binding insights and conformational consequences of the differential activity Here, using computational methods, we investigate the interacting determinants of CBD in two closely From our detailed characterization, we found particular interacting loci in the binding sites of the

GPCR scientists, translational pharmacologists, biotech drug discovery teams, and decision-makers who

This lesson reframes enzyme interaction not as background noise, but as a core pharmacological event. And responsible for countless drug–drug interactions. When Inhibition Becomes Activation Not all enzyme interactions are suppressive. Kenakin Content trusted by biotech, pharma, and academia 💎 $2999/year — one conference cost = a full Kenakin with your own enzyme or GPCR interaction puzzles.

September 2022 Ginsenoside Rg5 allosterically interacts with P2RY12 and ameliorates deep venous thrombosis

September 2022 GPCR/endocytosis/ERK signaling/S2R is involved in the regulation of the internalization Our results showed that the inhibition of cellular respiration hindered the internalization of F-Hst1 Overall, phagocytosis, CME, GPCR, ERK signaling, and S2R/TMEM97 are involved in the internalization of The inhibition of either internalization or mitochondria-targeting of Hst1 could significantly compromise

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We are able to identify the interaction of membrane cholesterols with definite sites and domains within We show that cholesterol interactions with the transmembrane domain TMD, unlike those with the cysteine-rich Notably, a few persistent interactions of cholesterol with lower TM cholesterol-binding domains are governed We have also reported the interaction of phosphatidylinositol 4-phosphate with the intracellular region The movement of these TM helices could possibly be a consequence of interactions involving the extracellular

August 2022 A new Kunitz-type snake toxin family associated with an original mode of interaction with and non-active V2R Kunitz peptides highlighted five positions, among which four are involved in V2R interaction We finally determined that eight positions, part of these two loops, interact with the V2R.

Multiple 14-3-3 isoforms exist, and a GPCR can differentially interact with different 14-3-3 isoforms

September 2022 CCL25/CCR9 interaction promotes the malignant behavior of salivary adenoid cystic carcinoma signaling pathway "Background CC chemokine receptor 9 (CCR9), an organ-specific chemokine receptor, interacts Western blot and RT–qPCR assays were carried out to measure the downstream factors of the interaction

GPCRs Are Optimal Regulators of Complex Biological Systems and Orchestrate the Interface between Health

G protein-coupled receptor interactions and modification of signalling involving the ghrelin receptor 1a (GHSR1a) is intriguing because of its potential as a therapeutic target and its diverse molecular interactions In all cases, the receptor interaction changes downstream signalling and the responses to receptor agonists

resonance (NMR) spectroscopy allows the determination of atomic-level information on intermolecular interactions In particular, we focus on the application of on-cell NMR spectroscopy to characterize ligand interactions

This is a highly prestigious international award – exemplified by the fact that other winners this year are the co-founders of BioNTech for their invention of the (Pfizer) Covid vaccine."

We uncovered a novel neuroprotective mechanism involving interaction between neurotrophic factor-α1 ( Co-immunoprecipitation and pull-down assays confirmed interaction between NFα1/CPE and 5-HTR1E and 125I Molecular dynamics studies revealed that NF-α1/CPE interacts with 5-HTR1E via 3 salt bridges, stabilized Thus, NF-α1/CPE uniquely interacts with serotonin receptor 5-HTR1E to activate the β-arrestin/ERK/CREB

This Week’s GPCR Intelligence: From Set-Point Pharmacology to No-Wash Internalization Assays This week Upcoming events:  47th Symposium on Hormones & Cell Regulation; new approach to GPCR internalization Target protected agonism:  Internalized MT2 signaling escapes AGRP antagonism—unlike α-MSH. GPCR scientists, translational pharmacologists, biotech discovery teams, and decision-makers who need tools, translational strategy, classified updates, and curated jobs—trusted by scientists, teams, and biotech

When pharmacologists misinterpret how an antagonist interacts with its receptor, the consequences ripple

biased signaling through ligands that stabilize receptor conformations and favor selective transducer interactions examine an additional mechanism: intracellular modulators that bind directly at receptor–transducer interfaces These systems are used here as resolved examples of how interface binding can stabilize specific signaling Interface-directed ligands introduce a second control layer for selectivity alongside receptor conformations and abolishing constitutive activity through a direct interface mechanism.

βarrs) play multifaceted roles in the function of G protein-coupled receptors (GPCRs). βarrs typically interact However, the effects of the C tail- and TM core-mediated interactions on the conformational activation Here, we show the conformational changes for βarr activation upon the C tail- and TM core-mediated interactions Our NMR analyses demonstrated that while the C tail-mediated interaction alone induces partial activation exists in equilibrium between basal and activated conformations, the TM core- and the C tail-mediated interactions