GRB2 _ ASH Control Peptide
- Known as:
- GRB2 _ ASH Control Peptide
- Catalog number:
- AP13277CP-N
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- GRB2 _ ASH Control Peptide
Related genes to: GRB2 _ ASH Control Peptide
- Gene:
- GRB2 NIH gene
- Name:
- growth factor receptor bound protein 2
- Previous symbol:
- -
- Synonyms:
- NCKAP2
- Chromosome:
- 17q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-03-04
- Date modifiied:
- 2016-10-05
Related products to: GRB2 _ ASH Control Peptide
Related articles to: GRB2 _ ASH Control Peptide
- The biological function of intrinsically disordered proteins is frequently coupled to short linear motifs, which serve as protein binding sites. This goes often hand in hand with local transient structural element formation. The intrinsically disordered C-terminal region of the multi-site docking protein Grb2-associated binder 1 (Gab1) contains several well-characterized phosphotyrosine pairs, whereas the Tyr162 and Tyr183 epitopes have remained practically unstudied. Here, we combine computational prediction, circular dichroism and high-resolution NMR spectroscopy (chemical shift and relaxation analyses) to structurally characterize a Gab1 fragment containing residues 142-203. The here determined NMR structure shows an α-helix for residues Pro180 to Ile187, with Tyr183 positioned centrally, while all other parts of the fragment, including the region around Tyr162, are disordered. This helical conformation is maintained upon changes in pH, variation of peptide lengths and phosphorylation status. The inherent helix around Tyr183 distinguishes the local structural environment of Tyr162 and Tyr183 within the intrinsically disordered Gab1 tail and provides a structural framework for future studies on interaction partners and potential functional roles of this structural motif. - Source: PubMed
Dietrich AnneLewitzky MarcGruber TobiasBalbach JochenFeller Stephan MWeininger Ulrich - The occurrence of hepatic fibrosis (HF) is closely related to the activation of hepatic stellate cells (HSCs), but the epitranscriptional regulatory mechanisms involved have not been fully elucidated. This study aims to explore the role and molecular mechanisms of the m6A reader protein IGF2BP2 in HSC activation and HF. - Source: PubMed
Publication date: 2026/07/27
Hu YouwenXiao Yangyang - In non-small cell lung cancer (NSCLC) with anaplastic lymphoma kinase (ALK) rearrangement, bypass signaling activation commonly leads to resistance against alectinib. Identifying key molecular targets that integrate signals from resistance-driving kinases is crucial for overcoming this resistance. However, these targets have not yet been identified. - Source: PubMed
Publication date: 2026/07/23
Chen HengyiLin CaiyuHu ChenLi WenHe Yong - Long-read RNA sequencing enables isoform-resolved transcriptomics, but library preparation introduces systematic biases that shape biological interpretation. We benchmarked Oxford Nanopore's two protocols-PCR-cDNA and direct RNA-using SKMM2 myeloma cells stimulated with interleukin-6 (IL-6) and ERCC synthetic spike-ins. Direct RNA produced longer, higher-quality reads and more high-confidence isoforms, but showed pronounced 5' coverage loss. PCR-cDNA yielded shorter fragments with 3' underrepresentation, detecting more low-abundance transcripts at reduced confidence. Protocol-specific biases had major consequences: differential expression analysis revealed limited overlap in IL-6-responsive genes, and pathway enrichment was broader in direct RNA. At the isoform level, differential transcript usage was almost entirely protocol-specific, with case studies (e.g. RPL22L1, GRB2, RNF220) illustrating concordance and divergence. ERCC controls confirmed these biases as technical rather than biological. Together, our results show that while both methods provide accurate gene-level quantification, transcript-level conclusions depend critically on protocol choice, highlighting the need for careful selection in long-read transcriptomics. - Source: PubMed
Publication date: 2026/07/15
Lane Rebecca ECalcutt EleanorSrinivasan AnandagopalGamble VickiOppermann UdoSun JianfengCribbs Adam P - Human parvovirus B19 infects erythroid progenitor cells and inhibits erythropoiesis. The small 11-kDa (s11-kDa) protein of the virus interacts with the host adaptor Grb2 (growth factor receptor-bound protein 2) and suppresses downstream kinase phosphorylation to promote viral genome replication; however, the underlying mechanism remains unclear. Here, we show that s11-kDa competitively disrupts the Grb2-SOS (Son of Sevenless) interaction by binding to the N-terminal SH3 domain of Grb2. Structural modeling indicated that the proline-rich region of the s11-kDa protein engage Grb2 molecules, potentially generating a high-affinity interaction that blocks SOS binding. These findings revealed a sophisticated viral replication strategy mediated by a viral accessory protein. - Source: PubMed
Publication date: 2026/07/16
Kimura SakikaUriu KeiyaArakawa MasashiEbina HirotakaMorita Eiji