Ask about this productRelated genes to: BCL2L1 Blocking Peptide
- Gene:
- BCL2L1 NIH gene
- Name:
- BCL2 like 1
- Previous symbol:
- -
- Synonyms:
- BCLX, BCL2L, Bcl-X, bcl-xL, bcl-xS, PPP1R52
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1997-10-30
- Date modifiied:
- 2016-01-13
Related products to: BCL2L1 Blocking Peptide
Related articles to: BCL2L1 Blocking Peptide
- selection and directed evolution technologies such as mRNA display, explore large libraries (≥10 variants) and generate thousands to millions of functional polypeptide ligands to a variety of targets. Denoising diffusion implicit machine learning models (DDIMs) trained using display-derived deep sequencing data can greatly expand these functional sequences beyond what is accessible experimentally. However, methods are needed to predict peptide properties such as binding free energies (ΔG°). Here, we applied machine learning methods to predict binding free energies of both experimental and DDIM-generated peptide ligands against a target of interest, the oncogenic protein Bcl-x . To do this, we trained a Closed-form Continuous (CfC) neural network using a dataset of 15,700 peptide ligands where pairs of sequences and their corresponding binding free energies (ΔG°) were used as inputs. This type of model was chosen due to its ability to represent irregular series. The resulting CfC model accurately predicts the rank order, within error, and binding free energies (ΔG°) for both experimental and DDIM-generated peptides, identifying five DDIM-generated peptides with single-digit picomolar affinities. Combining trained DDIM and CfC models offers a unified route to expand the scope of experimental ligand discovery, predict the molecular properties of both experimental and generated ligands, and highlights the utility of large quantitative datasets for making accurate predictions of high-affinity peptide candidates. - Source: PubMed
Publication date: 2026/05/08
Leaf Colin MQi PearlGandhi Yash PragneshJalali-Yazdi FarzadOng Justin NTakahashi Terry TKalia Rajiv KRoberts Richard W - This study aimed to systematically clarify the therapeutic effects and underlying mechanisms of Yiqi Huoxue Formula (YQHXF) against cerebral ischemia-reperfusion injury (CIRI) by integrating bioinformatics, network pharmacology, and in vitro/in vivo experiments. - Source: PubMed
Publication date: 2026/05/12
Zhang TiantianWang JinxiLi JiaminLiang YinshengTang ShuzeHu GuohengOu Liang - Nuclear factor kappa B (NF-κB) signaling plays a central role in inflammation, immunity, cell survival, and cancer progression. Its constitutive activation is frequently observed in breast cancer, contributing to tumor growth, treatment resistance, and metastasis. MicroRNAs (miRNAs) are key post-transcriptional regulators of gene expression and may modulate NF-κB signaling in a subtype-specific or -independent manner. The aim of the study was to identify miRNAs that may potentially regulate the activity of genes associated with NF-κB signaling across five molecular subtypes of breast cancer in Polish women. Tumor and matched normal tissue samples were collected from 405 patients with five breast cancer subtypes: luminal A ( = 130), HER2-negative luminal B ( = 100), HER2-positive luminal B ( = 96), non-luminal HER2-positive ( = 36), and triple-negative breast cancer (TNBC, = 43). Expression profile of selected NF-κB-related genes were evaluated using mRNA microarrays and RT-qPCR. Protein levels were assessed by ELISA. Candidate regulatory miRNAs were identified via miRNA microarrays and validated using the miRDB database. A consistent upregulation of , , , , , , , and was observed across all subtypes, suggesting activation of canonical NF-κB signaling. Downregulation of specific miRNAs, miR-1297 and miR-30a (targeting ), miR-134 (), miR-125b (), and miR-4329 (), may contribute to this deregulation. For , , , and , no regulatory miRNAs meeting our criteria were identified. Our study reveals a subtype-independent activation of the canonical NF-κB signaling pathway in breast cancer, underpinned by consistent upregulation of key components (at both the transcript and protein levels. Dysregulation of specific miRNAs likely contributes to this altered gene expression. These findings suggest the presence of a common NF-κB-driven oncogenic program across molecular subtypes, with potential implications for developing miRNA-based therapeutic strategies targeting inflammation, survival signaling, and treatment resistance in breast cancer. - Source: PubMed
Publication date: 2026/04/30
Mitka-Krysiak ElżbietaKról-Jatręga KatarzynaOssowski PiotrZmarzły NikolaBereza KrzysztofOrdon PawełSirek TomaszSirek AgataBoroń KacperBoroń DariuszWyrobiec GrzegorzSzczepanik TomaszSkorek MartaGrabarek Beniamin Oskar - Programmed cell death 4 (PDCD4) protein is a tumour suppressor protein that inhibits mRNA translation by inhibiting RNA helicase, eukaryotic initiation factor 4A (eIF4A). We have previously reported that PDCD4 interacts with the internal ribosome entry site (IRES) element of B-cell lymphoma extra-large (Bcl-xL) mRNA and inhibits its IRES-mediated translation initiation. S6 kinase (S6K)-mediated phosphorylation of PDCD4 activates its degradation and derepresses IRES-mediated translation initiation of Bcl-xL mRNA. eIF3F (one of the subunits of eIF3 complex) was reported to recruit S6K to phosphorylate eIF3G. Therefore, we investigated the possibility of co-regulation of PDCD4 and eIF3F by S6K and the regulation of IRES-mediated translation initiation by PDCD4-eIF3F. Here, we demonstrated that PDCD4 interacts with several subunits of eIF3. Specifically, eIF3F directly interacts with PDCD4 in an RNA-independent manner. Depletion of PDCD4 in glioblastoma (GBM) cells resulted in decreased levels of certain eIF3 subunits, including eIF3F. Additionally, depletion of eIF3F from GBM cells decreased the levels of PDCD4 protein. We also showed that PDCD4 and eIF3F directly interact with Bcl-xL RNA independently of each other. By performing IRES reporter, polysome profiling assays and EMSA we have demonstrated that eIF3F regulates IRES-mediated translation of Bcl-xL mRNA, likely via its interaction with PDCD4. - Source: PubMed
Publication date: 2026/04/29
Hegde VedaSharma Divya KPatel HarshilNarasimha Pavan LakshmiLuddu JasonMubaya RebeccaHolcik MartinThakor Nehal - Intrinsic apoptosis is a form of cell death which is activated, executed, and inhibited by the Bcl-2 protein family. The structural basis of the inhibition mechanisms remains elusive. Here, we characterize the ensemble structural model of the inhibitory Bcl-xL/tBid complex at the mitochondrial membrane by probing interresidue distances and dynamic solvent accessibilities complemented by integrative modeling and molecular dynamics simulations. We show that Bcl-xL and tBid form a heterodimer anchored to the membrane by the C-terminal helix of Bcl-xL. The BH3 domain of tBid is wedged between the exposed hydrophobic groove of Bcl-xL and the membrane headgroups, while tBid's C-terminal helices remain dynamically engaged with the bilayer. This dynamic architecture sheds light on the mechanism of indirect inhibition of apoptosis. - Source: PubMed
Publication date: 2026/05/11
Elsner ChristinaHanke AntonVadas OscarGervasio Francesco LuigiBordignon Enrica