The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is unambiguously human growth factor receptor-bound protein 2 (GRB2; alias ASH; UniProt P62993), not a similarly named protein. It is a highly conserved, 217-amino-acid, approximately 25-kDa member of the GRB2/sem-5/DRK family with the canonical N-terminal SH3–central SH2–C-terminal SH3 architecture specified in the query. Thus, the supplied identity, organism, family, and InterPro domain annotations are mutually consistent with the literature. (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 5-6)
GRB2 is not an enzyme and therefore catalyzes no chemical reaction and has no enzymatic substrate specificity. Its primary function is to act as a modular, multivalent adaptor: the SH2 domain anchors GRB2 to phosphotyrosine-bearing receptors or scaffolds, whereas its two SH3 domains engage proline-rich effectors. The canonical consequence is recruitment of SOS1/2 to activated receptor complexes at the cytoplasmic face of the plasma membrane, where SOS catalyzes RAS GDP–GTP exchange and initiates RAF–MEK–ERK signaling. GRB2 also organizes Gab–PI3K–AKT signaling, receptor endocytosis, immune-receptor assemblies, and membrane-associated condensates. (wang2024theconfigurationof pages 2-4, malagrino2024grb2adynamic pages 2-3, wang2024theconfigurationof pages 9-11)
| Component | Verified identity / architecture | Principal ligand preference | Core molecular consequence | Principal cellular site |
|---|---|---|---|---|
| N-terminal SH3 (N-SH3) | One of two SH3 modules flanking the central SH2 domain in human GRB2 (UniProt P62993) | Proline-rich ligands, preferentially PxxPxR motifs; prominent partner: SOS1 | Recruits the SOS guanine-nucleotide exchange factor, enabling membrane-localized RAS-GDP→RAS-GTP exchange and MAPK signaling (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 2-3) | Cytosol in preassembled complexes; recruited to the cytoplasmic face of activated plasma-membrane receptors and signaling clusters |
| SH2 | Central phosphotyrosine-recognition module | Phosphotyrosine-containing sequences, commonly pYxN-type motifs on activated RTKs or phosphorylated adaptors; examples include EGFR Y1068/Y1086 and PDGFRβ Y716 (wang2024theconfigurationof pages 1-2, wang2024theconfigurationof pages 9-11) | Anchors GRB2 complexes to phosphorylated receptors/scaffolds, thereby coupling receptor activation to SOS–RAS–RAF–MEK–ERK and Gab–PI3K–AKT signaling (wang2024theconfigurationof pages 2-4, wang2024theconfigurationof pages 9-11) | Cytoplasmic face of the plasma membrane after receptor activation; also phosphorylated signaling complexes on endosomes |
| C-terminal SH3 (C-SH3) | Second SH3 module completing the N-SH3–SH2–C-SH3 architecture | Proline-rich ligands with preference for PxxxRxxKP/PxxRxxKP-like motifs; partners include Gab proteins and context-dependent Cbl/BTK-associated complexes (wang2024theconfigurationof pages 17-18, malagrino2024grb2adynamic pages 2-3) | Expands partner selectivity and multivalency, supporting PI3K/AKT coupling, receptor trafficking, immune-signaling assemblies, and formation of higher-order signaling networks (malagrino2024grb2adynamic pages 3-3, nocka2023stimulationofthe pages 11-13) | Cytosolic complexes and receptor-proximal plasma-membrane clusters; endocytic assemblies when coupled to receptor–Cbl trafficking |
| Full-length GRB2 adaptor | Human GRB2/ASH, UniProt P62993; conserved 217-aa, approximately 25-kDa nonenzymatic adaptor in the GRB2/sem-5/DRK family, organized as N-SH3–SH2–C-SH3 (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 5-6) | Simultaneously integrates phosphotyrosine-bearing proteins through SH2 and proline-rich effectors through SH3 domains | Provides no catalytic reaction of its own; instead bridges, concentrates, spatially organizes, and dynamically regulates signaling proteins, including SOS-dependent RAS activation, receptor downregulation, BTK activation, and membrane-condensate assembly (wang2024theconfigurationof pages 9-11, lin2022atwocomponentprotein pages 1-2, nocka2023stimulationofthe pages 1-2) | Predominantly cytosolic at rest; transiently enriched at the inner plasma membrane, receptor clusters/condensates, and endosomes after stimulation; context-dependent nuclear localization has also been reported (wang2024theconfigurationof pages 2-4) |
Table: Domain-level summary of human GRB2 (UniProt P62993), linking its ligand-recognition modules to molecular consequences and sites of action. GRB2 is an interaction adaptor rather than an enzyme.
Two 2024 reviews independently describe GRB2 as a conserved 217-residue adaptor comprising a central SH2 domain flanked by N- and C-terminal SH3 domains. This matches UniProt P62993 and the supplied GRB2_N_SH3, SH2, and GRB2_C_SH3 annotations. The protein belongs to an evolutionarily conserved adaptor family represented by mammalian GRB2/ASH, C. elegans SEM-5, and Drosophila DRK. (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 2-3, malagrino2024grb2adynamic pages 5-6)
The available full-length crystal structure was determined at 3.1 Å resolution. The domains are not merely independent binding cassettes: folding and biophysical studies indicate interdomain communication, transient misfolded species, and an interface through which SH2 stability influences C-SH3 refolding. Contemporary expert reviews therefore portray GRB2 as a dynamic and potentially allosteric adaptor, rather than a rigid molecular connector. (malagrino2024grb2adynamic pages 2-3)
A nomenclature warning is warranted: one 2024 review reverses N-/C-SH3 labels in parts of its residue description. The canonical N-to-C arrangement—N-SH3, SH2, C-SH3—is used here because it agrees with UniProt P62993 and the broader structural literature. (wang2024theconfigurationof pages 1-2)
The central SH2 domain recognizes phosphorylated tyrosine sequences, commonly represented as pY-x-N-x motifs. This interaction recruits GRB2 to activated receptor tyrosine kinases (RTKs) or phosphorylated docking proteins. Experimentally supported receptor sites include EGFR Tyr1068 as a principal direct site, EGFR Tyr1086 as a secondary site, and PDGFRβ Tyr716; EGFR Tyr1173 can recruit GRB2 indirectly through SHC. Other reported sites include SHC Tyr239/240/317, SHP2 Tyr542, FAK Tyr925, MET Tyr1356, and IRS1 Tyr891. (wang2024theconfigurationof pages 17-18, wang2024theconfigurationof pages 9-11)
The two SH3 domains have overlapping but nonidentical specificity. Current reviews summarize N-SH3 preference as PxxPxR, whereas C-SH3 favors approximately PxxxRxxKP/PxxRxxKP sequences. These are recognition preferences rather than absolute consensus rules, and affinity in the intact protein depends on multivalency and interdomain configuration. SOS is the canonical N-SH3-associated effector; Gab proteins and additional signaling or trafficking proteins engage one or both SH3 modules in context-dependent ways. (wang2024theconfigurationof pages 17-18, malagrino2024grb2adynamic pages 2-3)
The functional principle is therefore combinatorial: SH2 captures a phosphorylated upstream component while SH3 domains recruit downstream proline-rich partners. This bridges proteins that otherwise have no direct catalytic relationship and increases their local concentration, dwell time, and spatial organization. (malagrino2024grb2adynamic pages 2-3, lin2022atwocomponentprotein pages 1-2)
The mechanistic precision is important: GRB2 does not itself exchange the nucleotide or phosphorylate a substrate. Its role is to position and organize SOS near membrane-associated RAS. Consequently, GRB2 function is controlled by interaction topology, stoichiometry, dwell time, phosphorylation, and receptor trafficking rather than by an intrinsic catalytic rate. (wang2024theconfigurationof pages 1-2, lin2022atwocomponentprotein pages 1-2)
GRB2 is predominantly soluble and cytosolic before stimulation, frequently associated with proline-rich partners. Upon receptor phosphorylation it becomes enriched at the cytoplasmic face of the plasma membrane, where it forms transient RTK–GRB2–SOS assemblies or larger two-dimensional signaling clusters. It subsequently participates in endosomal receptor complexes and Cbl-dependent trafficking. Cytoplasmic, membrane, endosomal, and context-dependent nuclear pools have all been reported, but the best-established site of its primary growth-factor signaling function is the inner plasma-membrane surface. (wang2024theconfigurationof pages 2-4, wang2024theconfigurationof pages 9-11)
Localization is dynamic rather than constitutive. In a membrane reconstitution, phosphorylated EGFR tails and GRB2 formed visible condensates within approximately 2–3 minutes, stabilizing by about 10 minutes. Addition of 1 μM YopH phosphatase dispersed them within 1 minute, directly demonstrating reversible phosphotyrosine-dependent assembly. (lin2022atwocomponentprotein pages 3-3, lin2021atwocomponentprotein pages 22-26)
GRB2 binds Gab-family docking proteins and helps recruit them to activated receptors. Phosphorylated Gab then recruits PI3K and associated effectors, coupling RTKs to PI3K–AKT signaling. This is a parallel output to GRB2–SOS–RAS rather than evidence that GRB2 possesses PI3K activity. (wang2024theconfigurationof pages 2-4, malagrino2024grb2adynamic pages 3-3)
GRB2 can bind phosphorylated EGFR through SH2 while an SH3 domain engages proline-rich Cbl. This promotes receptor ubiquitination and endocytosis, giving GRB2 a dual role: it initiates receptor-proximal signaling but also helps terminate or reshape it through trafficking. (wang2024theconfigurationof pages 9-11)
In unstimulated cells, GRB2 can form a complex with FGFR2 through its C-terminal SH3 domain and the receptor’s proline-rich C terminus, restraining receptor phosphorylation and MAPK output. FGF stimulation increases kinase activity, promotes GRB2 Tyr209 phosphorylation and dissociation, and allows downstream signaling. Pulldown, fluorescence-lifetime imaging, and isothermal-titration calorimetry support direct SH3–FGFR2 binding; the oncogenic FGFR2 S252W variant loses this regulatory interaction. (wang2024theconfigurationof pages 11-12)
A 2023 eLife study showed that full-length GRB2 binds the 44-residue proline-rich linker of membrane-bound BTK independently of GRB2 SH2 phosphotyrosine recognition. In PIP3-containing reconstituted membranes, GRB2 substantially increased BTK autophosphorylation and phosphorylation of a PLCγ2 segment at Tyr753 and Tyr759. The proposed mechanism is release of BTK autoinhibition through multivalent GRB2 engagement, followed by recruitment of BTK into LAT-associated signaling clusters. (nocka2023stimulationofthe pages 11-13, nocka2023stimulationofthe pages 6-7, nocka2023stimulationofthe pages 1-2)
This was demonstrated with supported lipid bilayers, TIRF imaging, construct mapping, phosphotyrosine blots, mass spectrometry, and single-molecule tracking. GRB2 recruitment required membrane-bound BTK or its isolated proline-rich linker and was reversible upon excess unlabeled GRB2 wash, arguing against nonspecific aggregation. BTK activation by GRB2 required PIP3-containing vesicles. (nocka2023stimulationofthe pages 4-6, nocka2023stimulationofthe pages 6-7)
A major recent conceptual development is that GRB2 can function as a multivalent crosslinker in receptor-proximal condensates, not simply as a one-receptor/one-effector bridge. In a 2022 PNAS reconstitution, phosphorylated EGFR cytoplasmic tails recruited GRB2 at Tyr1068, Tyr1086, Tyr1148, and Tyr1173. GRB2–GRB2 interactions then drove a two-dimensional phase transition on a supported membrane, and the resulting assembly enhanced SOS-dependent RAS activation. (lin2022atwocomponentprotein pages 1-2)
GRB2 Tyr160 was critical for this crosslinking: Y160 phosphorylation or mutation disrupted dimerization and prevented EGFR–GRB2 condensation. Condensate morphology depended on EGFR-tail surface density, from isolated circular domains at lower density to percolating networks at higher density. Because phosphatase rapidly reversed assembly, these structures are dynamic signaling compartments rather than irreversible aggregates. (lin2022atwocomponentprotein pages 1-2, lin2022atwocomponentprotein pages 3-3, lin2021atwocomponentprotein pages 22-26)
The current expert interpretation is that such assemblies regulate signaling by increasing local concentration and membrane dwell time while remaining sensitive to phosphorylation and dephosphorylation. However, much of the quantitative evidence comes from purified-protein supported-membrane systems. Their existence and exact material properties in native human tissues therefore require cautious interpretation. (lin2022atwocomponentprotein pages 1-2, lin2021atwocomponentprotein pages 13-16)
GRB2 output is regulated at several levels:
Nocka and colleagues established a function beyond passive recruitment: GRB2 can relieve BTK autoinhibition and increase kinase output on PIP3 membranes. Key quantitative conditions included 1 μM BTK, 250 μM vesicles containing 4% PIP3, and a 0–10 μM GRB2 titration; a separate LAT-cluster experiment used 5.8 μM GRB2, 1.45 μM SOS proline-rich region, and 1 nM fluorescent BTK. The authors appropriately characterized blot-derived activity measurements as semiquantitative rather than reporting an unsupported exact fold increase. Published 26 April 2023 in eLife: https://doi.org/10.7554/eLife.82676. (nocka2023stimulationofthe pages 18-19, nocka2023stimulationofthe pages 15-17, nocka2023stimulationofthe pages 6-7, nocka2023stimulationofthe pages 1-2)
Two 2024 reviews synthesized structural and functional evidence and emphasized that GRB2 specificity emerges from domain dynamics, interdomain communication, multivalency, and context—not from three independent binding modules. This interpretation supports allosteric drug discovery at interdomain interfaces but remains a research strategy rather than a clinically validated modality. Wang et al., published 22 February 2024: https://doi.org/10.3390/biom14030259; Malagrinò et al., September 2024: https://doi.org/10.1016/j.bbrep.2024.101803. (wang2024theconfigurationof pages 17-18, malagrino2024grb2adynamic pages 2-3, malagrino2024grb2adynamic pages 5-6)
Recent work reviewed in 2024 reinforces that GRB2 connects RTKs not only to SOS but also to Gab proteins, SHC, SHP2, Cbl, FAK, MET, IRS1, dynamin, and other partners. This breadth explains why complete GRB2 inhibition may have substantial on-target toxicity and why interface- or context-selective modulation may be preferable to global blockade. (wang2024theconfigurationof pages 17-18, malagrino2024grb2adynamic pages 3-3)
GRB2 is frequently implicated in cancers driven by EGFR, MET, BCR–ABL, Gab proteins, or aberrant RAS/MAPK signaling. Associations have been reported in breast, lung, liver, ovarian, colorectal, and bladder cancers and chronic myeloid leukemia. These associations generally reflect altered expression or dependency on upstream/downstream signaling networks; they do not establish GRB2 as a recurrently mutated oncogenic enzyme. (malagrino2024grb2adynamic pages 3-3)
Peptides and small molecules have been developed against GRB2 SH2 or SH3 interfaces. One SH2-inhibitory peptide had an IC50 of 350 nM, yet showed no antiproliferative effect, illustrating the gap between biochemical binding inhibition and cellular efficacy. Poor permeability, competition with high-local-concentration interactions, network redundancy, and the need to preserve normal signaling remain major obstacles. (malagrino2024grb2adynamic pages 5-6)
The most clinically advanced GRB2-directed approach is not a domain inhibitor but BP1001, a liposomal antisense oligonucleotide designed to reduce GRB2 expression. A 2024 review reports that, in a small AML combination cohort receiving BP1001 with venetoclax and decitabine, 12 of 14 patients (86%) achieved complete remission and 2 of 14 (14%) partial remission. These figures are preliminary, derive from only 14 patients, and cannot isolate the contribution of BP1001 from the combination regimen; they should not be interpreted as definitive efficacy or regulatory approval of GRB2 targeting. (wang2024theconfigurationof pages 17-18)
GRB2 is widely used experimentally as a live-cell or biochemical reporter of activated RTKs, because its SH2-dependent recruitment marks receptor phosphotyrosine formation. GRB2–SOS, GRB2–Cbl, and GRB2–Gab interactions are also used to dissect pathway bias, receptor trafficking, resistance mechanisms, and condensate formation. These are established research implementations, whereas direct GRB2 therapeutics remain investigational. (wang2024theconfigurationof pages 11-12, wang2024theconfigurationof pages 9-11, lin2022atwocomponentprotein pages 1-2)
High-confidence conclusions: target identity; human species; 217-residue N-SH3–SH2–C-SH3 architecture; nonenzymatic adaptor function; phosphotyrosine and proline-rich recognition; RTK–GRB2–SOS–RAS/MAPK coupling; plasma-membrane recruitment; and roles in receptor trafficking. These are supported by convergent structural, biochemical, mutational, imaging, and reconstitution evidence. (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 2-3, wang2024theconfigurationof pages 9-11)
Strong but context-dependent conclusions: Gab–PI3K–AKT coupling, FGFR2 restraint, BTK activation, and GRB2-mediated membrane condensation. These mechanisms are experimentally supported but vary by receptor, cell type, stoichiometry, and membrane context. (wang2024theconfigurationof pages 2-4, wang2024theconfigurationof pages 11-12, nocka2023stimulationofthe pages 11-13, lin2022atwocomponentprotein pages 1-2)
Translationally preliminary conclusions: direct SH2/SH3 inhibitors, allosteric interdomain inhibitors, and GRB2 antisense combinations. No retrieved evidence establishes a broadly approved direct GRB2 drug, and the encouraging AML response statistics require confirmation in larger controlled studies. (wang2024theconfigurationof pages 17-18, malagrino2024grb2adynamic pages 5-6)
Human GRB2/P62993 is best annotated as a noncatalytic, multivalent signal-routing adaptor. Its central biochemical role is to convert receptor phosphorylation patterns into spatially organized effector recruitment. The canonical output is SOS localization and RAS/MAPK activation, but the same modular architecture also controls PI3K/AKT coupling, immune kinase activation, receptor endocytosis, and dynamic membrane signaling assemblies. Recent research has shifted the field’s view from a static molecular bridge toward a conformationally dynamic, allosterically coupled organizer whose function depends on membrane localization, multivalency, stoichiometry, and condensate-like assembly. That richer mechanism creates therapeutic opportunities, but GRB2’s ubiquity and network centrality make selectivity and toxicity central unresolved challenges.
References
(wang2024theconfigurationof pages 1-2): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(malagrino2024grb2adynamic pages 5-6): Francesca Malagrinò, Elena Puglisi, Livia Pagano, Carlo Travaglini-Allocatelli, and Angelo Toto. Grb2: a dynamic adaptor protein orchestrating cellular signaling in health and disease. Sep 2024. URL: https://doi.org/10.1016/j.bbrep.2024.101803, doi:10.1016/j.bbrep.2024.101803. This article has 27 citations and is from a peer-reviewed journal.
(wang2024theconfigurationof pages 2-4): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(malagrino2024grb2adynamic pages 2-3): Francesca Malagrinò, Elena Puglisi, Livia Pagano, Carlo Travaglini-Allocatelli, and Angelo Toto. Grb2: a dynamic adaptor protein orchestrating cellular signaling in health and disease. Sep 2024. URL: https://doi.org/10.1016/j.bbrep.2024.101803, doi:10.1016/j.bbrep.2024.101803. This article has 27 citations and is from a peer-reviewed journal.
(wang2024theconfigurationof pages 9-11): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(wang2024theconfigurationof pages 17-18): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(malagrino2024grb2adynamic pages 3-3): Francesca Malagrinò, Elena Puglisi, Livia Pagano, Carlo Travaglini-Allocatelli, and Angelo Toto. Grb2: a dynamic adaptor protein orchestrating cellular signaling in health and disease. Sep 2024. URL: https://doi.org/10.1016/j.bbrep.2024.101803, doi:10.1016/j.bbrep.2024.101803. This article has 27 citations and is from a peer-reviewed journal.
(nocka2023stimulationofthe pages 11-13): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
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(nocka2023stimulationofthe pages 1-2): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
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(lin2021atwocomponentprotein pages 22-26): Chun-Wei Lin, Laura M. Nocka, Brittany Stinger, Joey DeGrandchamp, Nugent Lew, Steven Alvarez, Henry Phan, Yasushi Kondo, John Kuriyan, and Jay T. Groves. A two-component protein condensate of egfr and grb2 regulates ras activation at the membrane. bioRxiv, Dec 2021. URL: https://doi.org/10.1101/2021.12.12.472247, doi:10.1101/2021.12.12.472247. This article has 3 citations.
(wang2024theconfigurationof pages 11-12): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(nocka2023stimulationofthe pages 6-7): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
(nocka2023stimulationofthe pages 4-6): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
(lin2021atwocomponentprotein pages 13-16): Chun-Wei Lin, Laura M. Nocka, Brittany Stinger, Joey DeGrandchamp, Nugent Lew, Steven Alvarez, Henry Phan, Yasushi Kondo, John Kuriyan, and Jay T. Groves. A two-component protein condensate of egfr and grb2 regulates ras activation at the membrane. bioRxiv, Dec 2021. URL: https://doi.org/10.1101/2021.12.12.472247, doi:10.1101/2021.12.12.472247. This article has 3 citations.
(nocka2023stimulationofthe pages 18-19): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
(nocka2023stimulationofthe pages 15-17): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.