ArticleProteins2008
Structure-based classification of 45 FK506-binding proteins.
Article in Proteins, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 51 citations in OpenAlex.
- Combining Magnetic Resonance Imaging with Systemic Monocyte Evaluation for the Implementation of GBM Management.International journal of molecular sciences · 2021Trial
- Unveiling Novel Molecular Candidate Targets of Loratadine, Raloxifene, and Sorafenib in Hepatocellular Carcinoma.International journal of molecular sciences · 2026Article
- Genome-Wide Identification and Bioinformatics Analysis of the FK506 Binding Protein Family in Rice.Genes · 2024Article
- Genome and GWAS analysis identified genes significantly related to phenotypic state ofHorticulture research · 2024Article
- Macrophage-infectivity potentiator ofFrontiers in immunology · 2023Article
- The Developmental and Genetic Architecture of the Sexually Selected Male Ornament of Swordtails.Current biology : CB · 2021Article
- Retinal Organoids derived from hiPSCs of an AIPL1-LCA Patient Maintain Cytoarchitecture despite Reduced levels of Mutant AIPL1.Scientific reports · 2020Article
- Article
- FKBP12 enhances sensitivity to chemotherapy-induced cancer cell apoptosis by inhibiting MDM2.Oncogene · 2017Article
- FKBP51 Immunohistochemical Expression: A New Prognostic Biomarker for OSCC?International journal of molecular sciences · 2017Article
- Nucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments.Scientific reports · 2017Article
- Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.Journal of medicinal chemistry · 2016Review
- The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease.Molecular neurobiology · 2016Review
- Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Microbiology and molecular biology reviews : MMBR · 2014Review
- Prolyl hydroxylase domain protein 2 (PHD2) binds a Pro-Xaa-Leu-Glu motif, linking it to the heat shock protein 90 pathway.The Journal of biological chemistry · 2013Article
- FK506 binding protein 51 positively regulates melanoma stemness and metastatic potential.Cell death & disease · 2013Article
- Article
- The emerging role of large immunophilin FK506 binding protein 51 in cancer.Current medicinal chemistry · 2011Review
- Crystal structure of the three FK506 binding protein domains of wheat FKBP73: evidence for a unique wFK73_2 domain.Journal of structural and functional genomics · 2010Article
- Genome-wide analysis of genes encoding FK506-binding proteins in rice.Plant molecular biology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The FK506-binding proteins (FKBPs) are a unique group of chaperones found in a wide variety of organisms. They perform a number of cellular functions including protein folding, regulation of cytokines, transport of steroid receptor complexes, nucleic acid binding, histone assembly, and modulation of apoptosis. These functions are mediated by specific domains that adopt distinct tertiary conformations. Using the Threading/ASSEmbly/Refinement (TASSER) approach, tertiary structures were predicted for a total of 45 FKBPs in 23 species. These models were compared with previously characterized FKBP solution structures and the predicted structures were employed to identify groups of homologous proteins. The resulting classification may be utilized to infer functional roles of newly discovered FKBPs. The three-dimensional conformations revealed that this family may have undergone several modifications throughout evolution, including loss of N- and C-terminal regions, duplication of FKBP domains as well as insertions of entire functional motifs. Docking simulations suggest that additional sequence segments outside FKBP domains may modulate the binding affinity of FKBPs to immunosuppressive drugs. The docking models also indicate the presence of a helix-loop-helix (HLH) region within a subset of FKBPs, which may be responsible for the interaction between this group of proteins and nucleic acids.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.