Ask about this productRelated genes to: FKBP1A antibody
- Gene:
- FKBP1A NIH gene
- Name:
- FKBP prolyl isomerase 1A
- Previous symbol:
- FKBP1
- Synonyms:
- FKBP-12, FKBP12, PKC12, PPIASE, FKBP12C
- Chromosome:
- 20p13
- Locus Type:
- gene with protein product
- Date approved:
- 1992-09-14
- Date modifiied:
- 2018-11-01
Related products to: FKBP1A antibody
Related articles to: FKBP1A antibody
- Tacrolimus (TAC) is recommended for the patients with drug tolerance or respond poorly to other conventional immunosuppressants in myasthenia gravis (MG), but its effectiveness is influenced by dose and genetic polymorphism. Studies suggest that HLA polymorphisms are significantly associated with susceptibility to MG, but the relationship between HLA and TAC efficacy in MG has not been explored. In this paper, we investigated the correlation between TAC therapeutic efficacy and HLA in different MG subgroups. HLA-C*03 was associated with a better response to TAC in patients with early-onset MG, generalized MG, and those with a high concentration of TAC. While HLA-A*11:01 showed poor responsiveness to TAC in generalized MG. Furthermore, computational docking was used to demonstrate the binding situation of HLA-A with the TAC binding protein FKBP1A. It showed that HLA-A*11:01 had a higher binding strength with FKBP1A than HLA-C*03, indicating that the combination of different types of HLA and FKBP1A may be one of the reasons affecting its therapeutic efficacy. This study highlights the influence of HLA on the efficacy of TAC among different MG subgroups, providing clues for precise treatment of MG with TAC. - Source: PubMed
Lv YuanzhiChen KangzhiLuo MengchuanOuyang YuzhenLi KailinLuo ZhaohuiYang Huan - Hepatocellular carcinoma (HCC) is a significant global health burden. Cancer cells often exhibit an imbalance in intracellular calcium homeostasis. This study aims to explore the relationship between calcium-related genes and the prognosis of HCC, and establish a prognostic model based on calcium-related genes. - Source: PubMed
Publication date: 2026/03/21
Chen YanlingMa YarongZhao GuoruiLi JianhaoZhang Guizhen - Our goal was to identify new environmental or genetic causes in heritable pulmonary arterial hypertension (HPAH) families outside the 18 known diagnostics PAH genes. PAH gene panel sequencing was performed for 47 HPAH families which revealed pathogenic variants in 39 families. Five of the remaining families agreed to whole exome sequencing and to fill in a drug and toxin exposure questionnaire. In Family 1 and 2, mother and daughter with HPAH carried a likely pathogenic variant in the CYBA gene and a variant of uncertain significance in the FKBP1A gene, respectively, following ACMG guidelines. In Family 3, we detected a likely pathogenic variant in the PTGR2 gene. These genes could play part in PAH pathogenesis but further functional analyses are required to corroborate these findings. In the remaining two families, we could not identify any plausible genetic cause. However, a father and son with PAH reported exposure to trichloroethylene, asbestos and tramadol in Family 4. In Family 5, two brothers with pulmonary veno-occlusive disease showed occupational toxin exposure. Thus, our findings indicate that not only a genetic predisposition but also environmental triggers should be investigated for HPAH patients. - Source: PubMed
Publication date: 2026/01/29
Shaukat MemoonaGrünig EkkehardHaas SimonHaas JanPanahi MohammadGranzow MartinLange Tobias JStadler StefanSommer NataschaDorfmüller PeterMeder BenjaminHarutyunova SatenikEgenlauf BenjaminXanthouli PanagiotaHinderhofer KatrinEichstaedt Christina A - The function of a protein is determined by its structure, which may change dynamically in response to post-translational modifications, interaction with other molecules, or environmental factors like temperature. Limited proteolysis-coupled mass spectrometry (LiP-MS) captures such structural alterations on a proteome-wide scale via the detection of altered protease susceptibility patterns of proteins. However, this technique has so far required cell lysis, which exposes proteins to non-native conditions and can disrupt labile interactions such as those occurring within biomolecular condensates. To study protein structures directly within cells, we developed in-cell LiP-MS. We optimized conditions for introduction of proteinase K into human cells using electroporation and validated that intracellular cleavage occurs. In-cell LiP-MS captured the known binding of rapamycin to FKBP1A within the cell. Moreover, it detected global protein structural alterations upon sodium arsenite treatment and captured the structural dynamics of hundreds of proteins from biomolecular condensates with peptide level resolution and within live human cells. The data allowed monitoring of structural alterations of individual sites on the involved proteins, such as known RNA-binding and intrinsically-disordered regions, and dissected the timing of the different events. We detected known (G3BP1) and novel structural alterations of proteins from stress granules as well as from nuclear speckles and validated alteration of nuclear speckles by fluorescence microscopy and of the protein SERBP1 by polysome profiling. Our dataset further provides a resource describing the structural changes of human proteins in response to a cellular stress leading to biomolecular condensation and pinpoints structurally altered regions. Comparison of LiP-based structural fingerprints before and after cell lysis revealed which human proteins are susceptible to structural change upon cell lysis, therefore guiding the design of future experiments requiring native protein structures. - Source: PubMed
Publication date: 2026/01/12
Elsässer FranziskaFlorea RobertaRäsch FelixZedan MostafaSen Nesli-EcePflästerer TimKleele TatjanaLoewith RobbieWeis Karstende Souza NataliePicotti Paola - Radiotherapy often causes severe and irreversible neural damage, including cognitive impairment and depression-like behaviors. Current mitigants are limited, with single-target molecules being ineffective and nanomedicines posing complexity and toxicity risks. Dragon's Blood (DB), a nontoxic, brown-red resin extracted from (Lour.) (S. C. Chen, China), possesses diverse pharmacological properties. Extensive studies demonstrated that the compounds in DB exhibit multiple therapeutic effects, including cardiovascular protection, promotion of blood circulation, and anti-inflammatory effect. Herein, DB's neuronal radiation mitigation effect and mechanism were investigated. In a whole-brain irradiation rat model, DB administration significantly alleviated radiation-induced anhedonia-like behavior, normalized calcium dyshomeostasis, restored mitochondrial membrane potential, mitigated dendritic spine loss, suppressed neuroinflammation (IL-1β and TNF-α), and preserved hippocampal cytoarchitecture. Brain tissue proteomics revealed 23 DB-modulated KEGG pathways, encompassing the glutamatergic/GABAergic synapse, synaptic plasticity, addiction-related pathways, calcium/cAMP signaling, and hormonal regulation. Ensemble analysis integrating proteomics, WGCNA, machine learning, and PPI pinpointed 24 DB radiation mitigation-related proteins. Among these, eight targets (Grin1, Gabra4, Grm2, Grm3, Grm7, Prkcb, Shank3, and Pak7) functioning via ligand-target interactions were dysregulated by radiation and restored by DB. Molecular docking identified three DB ingredients (socotrin-4'-ol, cinnabarone, and 2'-methoxysocotrin-5'-ol) interacted with all eight targets. Plasma proteomics further revealed radiation mitigation-related brain-enriched proteins (Mib1, Gucy1b1, Fkbp1a, Synj1, and Clasp2). PPI between these 5 plasma proteins and 24 brain proteins reveals DB's multitarget radiation mitigation effect on neurotransmission and synaptic regulation, neuroplasticity, and signaling transduction and cellular response. This work nominated DB and its key constituents as promising candidates for mitigating radiotherapy-induced neural injury. - Source: PubMed
Publication date: 2025/11/25
Li BoyangHan ChuZhang HanLi Bo