Relevant bibliographies by topics / FKBPs

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Academic literature on the topic 'FKBPs'

Author: Grafiati
Published: 10 January 2023
Last updated: 28 January 2023

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Journal articles on the topic "FKBPs"

1

Wang, Chin-Chou, Wan-Jou Shen, Gangga Anuraga, Yu-Hsiu Hsieh, Hoang Dang Khoa Ta, Do Thi Minh Xuan, Chiu-Fan Shen, Chih-Yang Wang, and Wei-Jan Wang. "Penetrating Exploration of Prognostic Correlations of the FKBP Gene Family with Lung Adenocarcinoma." Journal of Personalized Medicine 13, no. 1 (December 26, 2022): 49. http://dx.doi.org/10.3390/jpm13010049.

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The complexity of lung adenocarcinoma (LUAD), the development of which involves many interacting biological processes, makes it difficult to find therapeutic biomarkers for treatment. FK506-binding proteins (FKBPs) are composed of 12 members classified as conservative intracellular immunophilin family proteins, which are often connected to cyclophilin structures by tetratricopeptide repeat domains and have peptidyl prolyl isomerase activity that catalyzes proline from residues and turns the trans form into the cis form. Since FKBPs belong to chaperone molecules and promote protein folding, previous studies demonstrated that FKBP family members significantly contribute to the degradation of damaged, misfolded, abnormal, and foreign proteins. However, transcript expressions of this gene family in LUAD still need to be more fully investigated. In this research, we adopted high-throughput bioinformatics technology to analyze FKBP family genes in LUAD to provide credible information to clinicians and promote the development of novel cancer target drugs in the future. The current data revealed that the messenger (m)RNA levels of FKBP2, FKBP3, FKBP4, FKBP10, FKBP11, and FKBP14 were overexpressed in LUAD, and FKBP10 had connections to poor prognoses among LUAD patients in an overall survival (OS) analysis. Based on the above results, we selected FKBP10 to further conduct a comprehensive analysis of the downstream pathway and network. Through a DAVID analysis, we found that FKBP10 was involved in mitochondrial electron transport, NADH to ubiquinone transport, mitochondrial respiratory chain complex I assembly, etc. The MetaCore pathway analysis also indicated that FKBP10 was involved in "Ubiquinone metabolism", "Translation_(L)-selenoaminoacid incorporation in proteins during translation", and "Transcription_Negative regulation of HIF1A function". Collectively, this study revealed that FKBP family members are both significant prognostic biomarkers for lung cancer progression and promising clinical therapeutic targets, thus providing new targets for treating LUAD patients.
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Galat, Andrzej. "Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl cis/trans Isomerases (PPIase)." Biomolecules 9, no. 2 (February 11, 2019): 59. http://dx.doi.org/10.3390/biom9020059.

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In this technical note, we describe analyses of more than 15,000 sequences of FK506-binding proteins (FKBP) and cyclophilins, also known as peptidyl-prolyl cis/trans isomerases (PPIases). We have developed a novel way of displaying relative changes of amino acid (AA)-residues at a given sequence position by using heat-maps. This type of representation allows simultaneous estimation of conservation level in a given sequence position in the entire group of functionally-related paralogues (multigene family of proteins). We have also proposed that at least two FKBPs, namely FKBP36, encoded by the Fkbp6 gene and FKBP51, encoded by the Fkbp5 gene, can form dimers bound via a disulfide bridge in the nucleus. This type of dimer may have some crucial function in the regulation of some nuclear complexes at different stages of the cell cycle.
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Bultynck, Geert, Daniela Rossi, Geert Callewaert, Ludwig Missiaen, Vincenzo Sorrentino, Jan B. Parys, and Humbert De Smedt. "The Conserved Sites for the FK506-binding Proteins in Ryanodine Receptors and Inositol 1,4,5-Trisphosphate Receptors Are Structurally and Functionally Different." Journal of Biological Chemistry 276, no. 50 (October 11, 2001): 47715–24. http://dx.doi.org/10.1074/jbc.m106573200.

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We compared the interaction of the FK506-binding protein (FKBP) with the type 3 ryanodine receptor (RyR3) and with the type 1 and type 3 inositol 1,4,5-trisphosphate receptor (IP3R1 and IP3R3), using a quantitative GST-FKBP12 and GST-FKBP12.6 affinity assay. We first characterized and mapped the interaction of the FKBPs with the RyR3. GST-FKBP12 as well as GST-FKBP12.6 were able to bind ∼30% of the solubilized RyR3. The interaction was completely abolished by FK506, strengthened by the addition of Mg2+, and weakened in the absence of Ca2+but was not affected by the addition of cyclic ADP-ribose. By using proteolytic mapping and site-directed mutagenesis, we pinpointed Val2322, located in the central modulatory domain of the RyR3, as a critical residue for the interaction of RyR3 with FKBPs. Substitution of Val2322for leucine (as in IP3R1) or isoleucine (as in RyR2) decreased the binding efficiency and shifted the selectivity to FKBP12.6; substitution of Val2322for aspartate completely abolished the FKBP interaction. Importantly, the occurrence of the valylprolyl residue as α-helix breaker was an important determinant of FKBP binding. This secondary structure is conserved among the different RyR isoforms but not in the IP3R isoforms. A chimeric RyR3/IP3R1, containing the core of the FKBP12-binding site of IP3R1 in the RyR3 context, retained this secondary structure and was able to interact with FKBPs. In contrast, IP3Rs did not interact with the FKBP isoforms. This indicates that the primary sequence in combination with the local structural environment plays an important role in targeting the FKBPs to the intracellular Ca2+-release channels. Structural differences in the FKBP-binding site of RyRs and IP3Rs may contribute to the occurrence of a stable interaction between RyR isoforms and FKBPs and to the absence of such interaction with IP3Rs.
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McKeen, Hayley D., Donal J. Brennan, Shauna Hegarty, Fiona Lanigan, Karin Jirstrom, Christopher Byrne, Anita Yakkundi, Helen O. McCarthy, William M. Gallagher, and Tracy Robson. "The emerging role of FK506-binding proteins as cancer biomarkers: a focus on FKBPL." Biochemical Society Transactions 39, no. 2 (March 22, 2011): 663–68. http://dx.doi.org/10.1042/bst0390663.

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FKBPs (FK506-binding proteins) have long been recognized as key regulators of the response to immunosuppressant drugs and as co-chaperones of steroid receptor complexes. More recently, evidence has emerged suggesting that this diverse protein family may also represent cancer biomarkers owing to their roles in cancer progression and response to treatment. FKBPL (FKBP-like) is a novel FKBP with roles in GR (glucocorticoid receptor), AR (androgen receptor) and ER (oestrogen receptor) signalling. FKBPL binds Hsp90 (heat-shock protein 90) and modulates translocation, transcriptional activation and phosphorylation of these steroid receptors. It has been proposed as a novel prognostic and predictive biomarker, where high levels predict for increased recurrence-free survival in breast cancer patients and enhanced sensitivity to endocrine therapy. Since this protein family has roles in a plethora of signalling pathways, its members represent novel prognostic markers and therapeutic targets for cancer diagnosis and treatment.
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MO, Yin-yuan, J. SESHU, Dong WANG, and Louis P. MALLAVIA. "Synthesis in Escherichia coli of two smaller enzymically active analogues of Coxiella burnetii macrophage infectivity potentiator (CbMip) protein utilizing a single open reading frame from the cbmip gene." Biochemical Journal 335, no. 1 (October 1, 1998): 67–77. http://dx.doi.org/10.1042/bj3350067.

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FK506-binding proteins (FKBPs) have been identified in a variety of eukaryotic and prokaryotic organisms. Macrophage infectivity potentiator (CbMip, 23.5 kDa) protein of the obligate intracellular bacterium, Coxiella burnetii, was shown previously to belong to the family of FKBPs based on sequence homology and peptidyl-prolyl cis/trans isomerase (PPIase) activity. Further characterization of the cbmip gene has identified two additional proteins with molecular masses of 15.5 and 15.0 kDa that are synthesized, in addition to the 23.5 kDa CbMip, when expressed in Escherichia coli. Amino acid sequencing at the N-terminus combined with transcription and translation fusion expression revealed that the two proteins were synthesized from the same open reading frame of the cbmip gene, but starting at different internal translation start codons, probably by translational reinitiation. When the internal methionines serving as start sites were replaced with lysine by site-directed mutagenesis, the synthesis of 15.5 and 15.0 kDa proteins was abolished even though the synthesis of 23.5 kDa CbMip was intact. This confirmed that the 15.5 and 15.0 kDa proteins are indeed generated by translational reinitiation and are not degradation products of the 23.5 kDa protein. Like other FKBPs, both 15.5 and 15.0 kDa proteins exhibit PPIase activity. Because they share significant sequence homology with FKBPs and have a similar PPIase activity, 15.5 and 15.0 kDa proteins are designated as C. burnetiiFKBP (Cb-FKBP) analogues I and II, respectively. TnphoA mutagenesis demonstrated that whereas the large protein (CbMip) is secreted, Cb-FKBP analogues I and II are cytoplasmic, indicating that structural variations could allow for different subcellular compartmentalization of similar proteins. Western-blot analysis of lysates of purified C. burnetii using a CbMip-specific monoclonal antibody revealed the presence of a protein migrating at ≈ 15 kDa, indicating the presence of smaller Cb-FKBP analogue(s) in C. burnetii, although at much lower levels compared with 23.5 kDa CbMip. This unique gene organization seen with cbmip may provide the organism with a mechanism of efficient use of its limited genetic information to synthesize proteins that are structurally different yet functionally similar.
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Geisler, Markus. "Regulation von ABC-Transportern durch FKBPs." BIOspektrum 27, no. 2 (March 2021): 131–34. http://dx.doi.org/10.1007/s12268-021-1548-x.

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AbstractThe plant hormone auxin is distributed in the plant by a sophisticated network of importers and exporters, including members of the ABCB subclass of ATP-binding cassette (ABC) transporters. ABCB-mediated auxin transport is controlled by Twisted Dwarf1, a member of the FK506-binding protein (FKBP) family. Here, we summarize current knowledge on ABC transporter regulation by FKBPs, which seems to be conserved over kingdoms and ABC subfamilies arguing for conserved mechanism of plant and mammalian post-translational transporter regulation.
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Yadav, Ravi P., Lokesh Gakhar, Liping Yu, and Nikolai O. Artemyev. "Unique structural features of the AIPL1–FKBP domain that support prenyl lipid binding and underlie protein malfunction in blindness." Proceedings of the National Academy of Sciences 114, no. 32 (July 24, 2017): E6536—E6545. http://dx.doi.org/10.1073/pnas.1704782114.

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FKBP-domain proteins (FKBPs) are pivotal modulators of cellular signaling, protein folding, and gene transcription. Aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) is a distinctive member of the FKBP superfamily in terms of its biochemical properties, and it plays an important biological role as a chaperone of phosphodiesterase 6 (PDE6), an effector enzyme of the visual transduction cascade. Malfunction of mutant AIPL1 proteins triggers a severe form of Leber congenital amaurosis and leads to blindness. The mechanism underlying the chaperone activity of AIPL1 is largely unknown, but involves the binding of isoprenyl groups on PDE6 to the FKBP domain of AIPL1. We solved the crystal structures of the AIPL1–FKBP domain and its pathogenic mutant V71F, both in the apo form and in complex with isoprenyl moieties. These structures reveal a module for lipid binding that is unparalleled within the FKBP superfamily. The prenyl binding is enabled by a unique “loop-out” conformation of the β4-α1 loop and a conformational “flip-out” switch of the key W72 residue. A second major conformation of apo AIPL1–FKBP was identified by NMR studies. This conformation, wherein W72 flips into the ligand-binding pocket and renders the protein incapable of prenyl binding, is supported by molecular dynamics simulations and appears to underlie the pathogenicity of the V71F mutant. Our findings offer critical insights into the mechanisms that underlie AIPL1 function in health and disease, and highlight the structural and functional diversity of the FKBPs.
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Chambraud, Béatrice, Cillian Byrne, Geri Meduri, Etienne Emile Baulieu, and Julien Giustiniani. "FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story." International Journal of Molecular Sciences 23, no. 3 (February 3, 2022): 1738. http://dx.doi.org/10.3390/ijms23031738.

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The FK506-binding protein 52 (FKBP52) belongs to a large family of ubiquitously expressed and highly conserved proteins (FKBPs) that share an FKBP domain and possess Peptidyl-Prolyl Isomerase (PPIase) activity. PPIase activity catalyzes the isomerization of Peptidyl-Prolyl bonds and therefore influences target protein folding and function. FKBP52 is particularly abundant in the nervous system and is partially associated with the microtubule network in different cell types suggesting its implication in microtubule function. Various studies have focused on FKBP52, highlighting its importance in several neuronal microtubule-dependent signaling pathways and its possible implication in neurodegenerative diseases such as tauopathies (i.e., Alzheimer disease) and alpha-synucleinopathies (i.e., Parkinson disease). This review summarizes our current understanding of FKBP52 actions in the microtubule environment, its implication in neuronal signaling and function, its interactions with other members of the FKBPs family and its involvement in neurodegenerative disease.
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Liu, Fei, Xiao-Long Wei, Hao Li, Ji-Fu Wei, Yong-Qing Wang, and Xiao-Jian Gong. "Molecular Evolution of the Vertebrate FK506 Binding Protein 25." International Journal of Genomics 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/402603.

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FK506 binding proteins (FKBPs) belong to immunophilins with peptidyl-prolyl isomerases (PPIases) activity. FKBP25 (also known as FKBP3) is one of the nuclear DNA-binding proteins in the FKBPs family, which plays an important role in regulating transcription and chromatin structure. The calculation of nonsynonymous and synonymous substitution rates suggested that FKBP25 undergoes purifying selection throughout the whole vertebrate evolution. Moreover, the result of site-specific tests showed that no sites were detected under positive selection. Only one PPIase domain was detected by searching FKBP25 sequences at Pfam and SMART domain databases. Mammalian FKBP25 possess exon-intron conservation, although conservation in the whole vertebrate lineage is incomplete. The result of this study suggests that the purifying selection triggers FKBP25 evolutionary history, which allows us to discover the complete role of the PPIase domain in the interaction between FKBP25 and nuclear proteins. Moreover, intron alterations during FKBP25 evolution that regulate gene splicing may be involved in the purifying selection.
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Pagani, Alessia, Mariateresa Pettinato, Alessandro Dulja, Silvia Colucci, Mariam Aghajan, Valeria Furiosi, Martina U. Muckenthaler, Shuling Guo, Antonella Nai, and Laura Silvestri. "Dissecting the Mechanisms of Hepcidin and BMP-SMAD Pathway Regulation By FKBP12." Blood 138, Supplement 1 (November 5, 2021): 2008. http://dx.doi.org/10.1182/blood-2021-152172.

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Abstract The BMP-SMAD pathway is activated when a dimeric ligand (BMP) interacts with a dimeric serine threonine kinase receptor (BMPRII) and triggers the activation of a dimeric BMP type I receptor (BMPRI). Catalytically active BMPRIs phosphorylate SMAD1/5/8 that, upon SMAD4 binding, translocate to the nucleus to regulate the expression of BMP target genes, including hepcidin. Hepcidin is the main regulator of iron homeostasis that controls body iron levels by binding and blocking the sole iron exporter ferroportin. In agreement, hepcidin expression is homeostatically activated by serum and liver iron, and its deficiency is a common hallmark of Hereditary Hemochromatosis (HH) and the major cause of iron overload in beta thalassemia. The components of the BMP-SMAD pathway relevant for hepcidin regulation are ALK2 and ALK3 (BMPRI); BMPR2 and ACVR2A (BMPRII), BMP2 and BMP6 (BMP ligands). Recently, we have identified the immunophilin FKBP12 as an inhibitor of hepcidin and demonstrated that FKBP12 binds ALK2 to avoid ligand-independent activation of the BMP-SMAD pathway. To investigate the mechanism of BMP-SMAD pathway and hepcidin regulation by FKBP12, we performed in vitro, ex vivo and in vivo studies. We found that FKBP12 sequestration by the immunosuppressive drug Tacrolimus (TAC) stabilizes ALK2-ALK2 homodimers and ALK2-ALK3 heterodimers in a transfected human hepatoma cell line. In addition, it increases the interaction of ALK2 with ACVR2A and BMPR2. To investigate the role of FKBP12 on BMP-SMAD signaling, BMPRI and II were silenced in murine primary hepatocytes. Despite FKBP12 co-immunoprecipitates only with ALK2, silencing of Alk2 and Alk3 completely blunts TAC-mediated BMP-SMAD pathway activation, suggesting that FKBP12 functionally interacts also with ALK3. Acvr2a silencing impairs TAC-dependent hepcidin upregulation, whereas Bmpr2 silencing does not. As expected, Fkbp12 silencing abrogates hepcidin upregulation by TAC, confirming the main role of this immunophilin in hepcidin regulation. In vivo, TAC treatment upregulates hepcidin in wild type and HH mouse models, but surprisingly, Fkbp12 mRNA downregulation by ASOs does not. Interestingly, Fkbp 2, 4 and 8 are highly expressed in murine hepatocytes and, according to literature data, are able to bind to TAC. Of note, Fkbp12 is the least expressed immunophilin in murine primary hepatocytes. To further investigate the FKBPs involved in TAC-dependent hepcidin regulation, Fkbp2, 4 and 8 were knockdown in murine primary HCs that were then treated with TAC. The TAC effect is preserved in siFkbp2- and siFkbp4-derived HCs, but abolished when Fkbp8 was downregulated. Overall these data suggest that: 1) FKBP12 regulates BMP-SMAD signaling by favoring ALK2-ALK3 homo and heterodimerization, and interaction with BMPRII in the absence of ligands; 2) TAC-mediated hepcidin upregulation is dependent upon ALK2, ALK3, ACVR2A, FKBP12 and FKBP8. 3) In vivo, TAC treatment upregulates hepcidin whereas Fkbp12 silencing does not, suggesting the existence of redundancy between the different FKBPs. Further studies are needed to dissect the role of FKBP8 in BMP-SMAD pathway and hepcidin regulation. Disclosures Aghajan: Ionis Pharmaceuticals, Inc.: Current Employment. Muckenthaler: Silence Therapeutics: Research Funding. Guo: Ionis Pharmaceuticals, Inc.: Current Employment.
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Dissertations / Theses on the topic "FKBPs"

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Fabian, Anne-Katrin [Verfasser], and Christoph [Akademischer Betreuer] Turck. "InterAKTion with FKBPs : modulation of the Akt/mTOR pathway by FKBPs / Anne-Katrin Fabian ; Betreuer: Christoph Turck." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2013. http://d-nb.info/1132061113/34.

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Xiol, Jordi. "Etudes fonctionnelles sur les composants de la voie des piRNAs MOV10L1 et FKBP6." Phd thesis, Université de Grenoble, 2011. http://tel.archives-ouvertes.fr/tel-00664995.

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Les piwi-interacting RNAs (piRNA) interagissent avec les protéines qui font partie de la branche PIWI de la famille des Argonautes. Ils participent à la répression des transposons dans la ligne germinale. Chez la souris, les protéines PIWI sont indispensables pour la fertilité des mâles et sont responsables de la méthylation de l'ADN au niveau des promoteurs des transposons. Les piRNA sont produis à partir de deux mécanismes: la biogenèse primaire et le cycle d'amplification ping-pong. Nous avons fait des études fonctionnelles sur deux protéines qui participent à la voie des piRNA: l'hélicase d'ARN MOV10L1 et l'immunophiline FKBP6. Nous avons décrit le rôle de MOV10L1 en tant que facteur de biogenèse primaire. La disruption génétique du domaine hélicase de MOV10L mène à une activation des transposons et à une perte de la méthylation de l'ADN. Ainsi, les piRNA ne sont pas produits chez le mutant, ce qui suggère que MOV10L1 est essentielle pour la biogenèse des piRNA. Tdrd1 interagit avec les protéines PIWI et joue un rôle dans la voie des piRNA en recrutant quelques facteurs à partir de son domaine MYND N-terminal. Nous avons montré que le domaine MYND de Tdrd1 interagit avec FKBP6, une protéine qui appartient à une famille d'isomérases de prolines qui sont présentes dans des complexes de chaperonnes. Les études biochimiques réalisées indiquent que FKBP6 est inactive et qu'elle utilise son domaine isomérase comme un module structural qui interagit avec les protéines PIWI, alors qu'elle interagit avec Hsp90 avec son domaine TPR. L'analyse d'une souris mutante pour fkbp6 a révélé une dérépression des transposons et une perte de la méthylation de l'ADN, mais peu d'effets sur la biogenèse primaire. Ces résultats sont en accord avec un rôle de FKBP6 en aval de Tdrd1, et nous pouvons penser que ce rôle pourrait être le recrutement de Hsp90 pour participer au cycle d'amplification ping-pong.
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Garrido, Marine. "Identification de la protéine chaperonne FKBP7 comme une nouvelle cible thérapeutique dans le cancer de la prostate résistant à la chimiothérapie." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS181/document.

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Le cancer de la prostate est le second cancer diagnostiqué chez les hommes dans le monde. Malgré le développement de nouveaux traitements au cours de ces cinq dernières années, les chimiothérapies par taxanes, docetaxel et cabazitaxel, restent des traitements de référence dans la prise en charge des patients atteints de cancer de la prostate métastatique résistant à la castration. Cependant, des résistances primaires et acquises émergent chez environ la moitié des patients. C’est pourquoi, il est urgent de découvrir et de comprendre les mécanismes de résistance aux taxanes afin d’identifier de nouvelles cibles thérapeutiques. En effet, de nouvelles thérapies ciblées peuvent émerger de la compréhension des voies de signalisation impliquées dans le cancer de la prostate pour contourner la chimiorésistance et améliorer les traitements. Les protéines chaperonnes jouent un rôle clef dans la régulation de l’homéostasie cellulaire et dans le développement de résistance aux traitements. Elles constituent donc des cibles thérapeutiques potentielles pour contourner la chimiorésistance. En réalisant un criblage fonctionnel par siARN à partir de profils d’expression génique, nous avons identifié FKBP7, une chaperonne moléculaire encore jamais étudiée chez l’homme, impliquée dans la résistance au docetaxel et au cabazitaxel. FKBP7 est surexprimée dans les tumeurs de la prostate et son expression est corrélée avec la récurrence chez les patients ayant reçu du docetaxel en thérapie néoadjuvante. De plus, FKBP7 est surexprimée dans des lignées cancéreuses prostatiques résistantes aux taxanes et son expression est nécessaire à leur croissance in vitro et à la croissance tumorale dans un modèle murin de résistance au docetaxel. Par des approches de protéomique haut-débit, nous avons identifié la voie de signalisation régulée par FKBP7 qui est responsable de la survie des cellules chimiorésistantes. Enfin, nous proposons une stratégie thérapeutique pour contourner la chimiorésistance au docetaxel et au cabazitaxel en ciblant l’effecteur moléculaire en aval de FKBP7
Prostate cancer is the second cancer diagnosed among men worldwide. Beside approval of new therapies in the last five years, chemotherapeutic agents, docetaxel and cabazitaxel taxanes remain key treatments for metastatic castration resistant prostate cancers. However, primary and acquired resistance to taxanes still emerged in about half of patients. There is therefore an urgent need to discover and understand the taxane resistance mechanisms in order to identify new therapeutic targets. Indeed, targeted therapies that exploit the signaling pathways involved in prostate cancer are required to overcome chemoresistance and improve treatment outcomes. Molecular chaperones play a key role in the regulation of cellular homeostasis and the development of treatment resistance, and are promising therapeutic targets. Using high throughput siRNA functional screening based on a gene expression signature, we identified FKBP7, involved in acquired resistance to docetaxel and cabazitaxel. FKBP7 is a molecular chaperone that has not been studied in human so far. FKBP7 is overexpressed in prostate tumors and its expression is correlated with recurrence in patients who received docetaxel as neoadjuvant therapy. Moreover, FKBP7 is upregulated in taxane resistant prostate cancer cell lines and its expression sustains their growth in vitro and in a mice model of Docetaxel resistance. Using a high throughput proteomic approach, we identified the signaling pathway regulated by FKBP7 which is responsible for the survival of chemoresistant cells. Finally, we proposed a promising therapeutic strategy to overcome both docetaxel and cabazitaxel chemoresistance by targeting the downstream effector of FKBP7
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Blair, Laura J. "Age-associated increases in FKBP51 facilitate tau neurotoxicity." Scholar Commons, 2014. https://scholarcommons.usf.edu/etd/5185.

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Tau is a protein which regulates microtubule stability and is heavily involved in axonal transport. This stability is dynamically controlled in part by over 40 phosphorylation sites across the tau protein which allows for binding and release from the microtubules. However, if abnormal hyperphosphorylation occurs, tau dissociates from the microtubules. Once released, the microtubules become unstable and the aberrant tau mislocalizes from the axon to the somatodendric compartment, where it aggregates. These aggregates are made of many pathological forms of tau including oligomeric species, paired helical filaments, and neurofibrillary tangles, all of which have associated toxicities. Tau pathology is a hallmark of Alzheimer's disease, one of over 15 diseases known as tauopathies which present with tau pathology, all of which lack effective treatments. Heat shock protein 90 kDa (Hsp90) is a major adenosine triphosphate (ATP)-dependent regulator of non-native proteins, like misfolded tau. Although Hsp90 is able to effectively refold and degrade many aberrant proteins, it has been associated with preserving aberrant tau. In fact, inhibiting the Hsp90 ATPase activity leads to the degradation of tau, which has been demonstrated in a number of models with the use of various Hsp90 inhibitors. However, there are many side-effects associated with the use of these inhibitors including toxicity and heat shock factor 1 (HSF1) activation. Although improvements on Hsp90 inhibitors are still in progress, this study explores targeting Hsp90 through a slightly different mechanism, by targeting Hsp90 co-chaperones. Hsp90 is involved in almost every pathway in each cell throughout the body. Co-chaperone proteins assist Hsp90 in these various processes, but are each only involved in a subset of the total Hsp90 interactome. Therefore, targeting Hsp90 co-chaperones could lead to improved efficacy, potency, and safety of drugs designed toward Hsp90 for the treatment of tauopathies. We previously showed one of these co-chaperones, FK506 binding protein 51 kDa (FKBP51), a tetratricopeptide repeat (TPR) domain containing immunophilin, coordinates with Hsp90 to regulate tau metabolism. More specifically, we found that increases and decreases in FKBP51 levels correlated with increases and decreases in tau levels, respectively. FKBP51 knockout mice have been extensively studied and have shown no negative phenotypes in these characterizations. In this study, we found that this mouse model has decreased endogenous tau levels. Furthermore, this study demonstrates that FKPB51 colocalizes with pathological tau in the AD brain, and synergizes with Hsp90 to preserve tau from proteasomal degradation. Additionally, FKBP51 overexpression in mouse model of tau pathology leads to the preservation of tau. We went on to characterize this accumulated tau as being neurotoxic and oligomeric in nature, while being low in silver positive, β-sheet structure. In the human brain, we found that FKBP51 is strikingly increased with aging and even further in the AD brain. In support of these findings, we also found age-associated decreased methylation in the FKBP5 gene, which encodes FKBP51. Moreover, we found that increasing levels of FKBP51 caused other co-chaperone to have reduced Hsp90 binding and led to tau preservation. This supports a model where age-related increases in FKBP51 lead to the preservation of misfolded tau species and ultimately disease. In order to model the high FKBP51 expression found in the aging brain, we generated the first FKBP5 overexpressing mouse model, which is tet-regulatable. This mouse, rTgFKBP5, was made by targeted, single insertion of the human FKBP5 gene into the HIP11 locus of the mouse genome crossed with CamKIIα tTa mice. We have now confirmed high FKBP51 levels in the forebrain and hippocampus of this mouse, which will serve as a testing platform for FKBP51 regulating drugs. Overall, this work exemplifies FKBP51 as an important regulator of tau metabolism through Hsp90. With the absence of a negative phenotype in mice ablated of FKBP51 and the development of this novel, FKBP51 overexpressing mouse model, strategies designed to decrease FKPB51 levels or to disrupt the FKBP51/Hsp90 complex could be relevant for the treatment of tauopathies, like AD.
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Annett, Stephanie Louise. "The role of FKBPL and its peptide derivatives in targeting stemness." Thesis, Queen's University Belfast, 2017. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.725332.

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FKBPL is a secreted protein with well-established anti-angiogenic activity and a novel therapeutic peptide, ALM201, derived from the protein has entered Phase l/ll clinical trial in ovarian cancer patients. Ovarian cancer is the most lethal gynaecologic cancer with a high incidence of recurrent chemo-resistant disease and this has been attributed to a subpopulation of cancer stem cells (CSCs), which escape standard therapies and drive metastatic spread. ALM201 binds to the cell surface receptor antigen, CD44, a classic marker of CSCs, and for the first time, we demonstrate ALM201's ability to target ovarian CSCs. Tumoursphere assays have demonstrated that ALM201 is effective at reducing ovarian CSCs in a range of cell lines and primary patient samples in vitro and reduced the CD44+CD117+ ovarian CSC subpopulation. Clonogenic assays suggest that ALM201 mediates ovarian CSC differentiation; a similar observation was previously noted in breast cancer. In vitro ALM201 displayed potent anti-CSC activity in the high grade serous (HGS) ovarian cancer cell line, OVCAR3, however, it displayed no anti-angiogenic or anti-CSC efficacy in in vivo models. In contrast, ALM201 treatment of Kuramochi xenografts resulted in significant growth delay and a 10 fold decrease in CSCs in in vivo experiments. Upon CD31/PAS staining, the Kuramochi xenografts displayed an extensive CD31+ vasculature network, which was disrupted by treatment with ALM201. On the other hand, the OVCAR3 xenografts had relatively few CD31+ blood vessels but had extensive PAS+ vasculogenic mimicry (VM) networks; which ALM201 did not target. Furthermore, OVCAR3 xenografts dramatically up regulated the inflammatory cytokines IL-6 and IL-8, in comparison to the Kuramochi xenografts, and as a result ALM201 had no effect on the CSC sub-population. In a tissue microarray of HGS ovarian cancer patients, high FKBPL expression correlated with an increase in progression free interval thus indicating a role for FKBPL as a prognostic biomarker in the clinic. Endocrine therapies are commonly used to prevent ER+ breast cancer release however, findings suggest that they may be increasing treatment resistant breast CSCs. FKBPLs preclinical peptide AD-01 has previously shown potent anti-CSC activity in the breast cancer setting and here we demonstrate its ability to abrogate endocrine enrichment of CSCs in both cell lines and patient samples. Furthermore, we demonstrate using in vivo limiting dilution models that ALM201 alone or in combination with tamoxifen was effective at delaying tumour recurrence by 12 days and 21 days, respectively. FKBPL and its peptide derivatives down regulate the DLL4/Notch pathway, a regulator of CSC self-renewal, thus indicating a novel mechanism of action. In the haemopoietic setting, ALM201 inhibited migration of chronic lymphocytic leukaemia (CLL) - like cell lines without inducing apoptosis. In an in vivo model of CLL, treatment of ALM201 resulted in a compartmental shift of the cells from the bone marrow to the peripheral blood and spleen. Furthermore, in vitro studies of acute lymphocytic leukaemia (AML) cell lines show that the combination of ALM201 and all trans retinoic acid (ATRA) significantly reduces cell viability, compared to ATRA alone. Analysis of AML cell morphology indicates that ALM201 may be inducing cellular differentiation and thus overcoming the characteristic maturation arrest of this disease. In summary, high FKBPL levels is associated with progression free survival in HGS ovarian cancer patients and the clinical FKBPL peptide, ALM201, effectively targets angiogenesis and CSCs in well-vascularised HGS ovarian cancer thus enhancing the efficacy of this agent in the clinic. In addition, we have demonstrated additional indications for ALM201 in treating endocrine resistance in breast cancer and a novel role in haematopoietic malignancies.
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Patel, Satyam Gunvantbhai. "Characterization of amygdalar Fkbp5 role in stress-induced anxiety-like behaviour." Thesis, University of Leicester, 2012. http://hdl.handle.net/2381/27663.

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The physiological response to excessively strong aversive stimuli – the stress response – is relatively maladaptive and leads to various psychopathologies such as anxiety disorders only in a minority of individuals. Our lab has previously shown that severe acute restraint stress heightens anxiety-like behaviour in wild-type but not in the extracellular serine protease, neuropsin, deficient mice. Dissecting molecular changes underlying genotypic differences, our microarray and qRT-PCR approaches revealed that the stress-induced upregulation of glucocorticoid receptor (GR) co-chaperone, Fkbp5, expression in the amygdala is significantly attenuated in neuropsin-/- mice compared to the wild-type mice and attenuated expression can be restored by bilateral intraamygdala injection of recombinant neuropsin. Further, blocking neuropsin cleavage of EphB2 with anti-EphB2 antibody suppressed only neuropsin-mediated but not corticosterone-driven upregulation of Fkbp5 expression in primary amygdala cultures unraveling novel neuropsin-dependent mechanism acting in synergy with the well characterized corticosterone pathway to mediate the robust stress-effect on Fkbp5 expression. Importantly, wild-type mice lacking amygdala specific Fkbp5 exhibit stress protective phenotype in unconditioned anxiety tests. Therefore, this study characterizes and concludes an indispensable role of amygdalar Fkbp5 in stressful episodes developing into anxiety disorders.
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Wiechmann, Tobias [Verfasser], and Mathias [Akademischer Betreuer] Schmidt. "Epigenetic mechanisms of fine-tuning FKBP5 gene expression / Tobias Wiechmann ; Betreuer: Mathias Schmidt." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2019. http://d-nb.info/1222436531/34.

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Acino, Erin Reese. "Transcriptional Regulation of the Mouse FKBP5 Gene by Progesterone and Glucocorticoid Receptor Binding." Thesis, The University of Arizona, 2010. http://hdl.handle.net/10150/146207.

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Steroid hormone receptors bind to DNA and interact with transcription-regulating proteins to affect a change in gene expression levels. However, questions remain about their choice of binding sites in vivo and their cooperation with other transcription factors. This experiment uses chromatin immuno-precipitation (ChIP) to attempt to identify progesterone and glucocorticoid receptor binding sites in the mouse FKBP5 gene. However, no sites were identified due to poor-quality sheared chromatin. Use of a circulating water bath to maintain low temperatures during sonication could improve consistency in future experiments, and more cellular material could increase the likelihood of successful immuno-precipitations.
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Neumann, Jacob Trevor. "THE ROLE OF ATP AND FK-506 BINDING PROTEIN IN THE COUPLED GATING OF SKELETAL RYANODINE RECEPTORS." OpenSIUC, 2011. https://opensiuc.lib.siu.edu/dissertations/348.

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During skeletal muscle stimulation, there is a summation of local events of Ca2+ release from the sarcoplasmic reticulum, known as Ca2+ sparks. Ca2+ sparks originate from groups of skeletal ryanodine receptors (RyR1) that activate and close in synchrony. This synchrony allows for the rapid and massive release of Ca2+ from the sarcoplasmic reticulum to initiate contraction and, more important, would provide a mechanism to terminate Ca2+ release under conditions where independent RyR1 are normally active. RyR1 mutations can result in abnormal intracellular Ca2+ signaling that is associated with numerous skeletal muscle disorders including malignant hyperthermia and central core disease. Therefore, investigating the mechanisms that control RyR1 function can help identify how these mutations cause deleterious Ca2+ handling. Currently, most published research on RyR1s gating utilizes single RyR1 reconstituted into planar lipid bilayers to test isolated RyR1. However, in vivo, arrays of RyR1 function in synchrony. Attempts to reconstitute RyR1s into planar lipid bilayers result in experiments that contain multiple channels, which under specific conditions may gate in synchrony, also known as coupled gating. Coupled RyR1 gating was first reported by A. Marks' laboratory and attributed to FK-506 binding protein 12 (FKBP12) associating with neighboring RyR1s the stabilization of RyR1-RyR1 interactions that promote coupled gating. Previous studies suggested that ATP is required for coupled RyR1 gating; however, the mechanism by which ATP promotes the coordinated activity of RyR1s has not been elucidated and is the focus of this thesis. Therefore, my hypothesis is that the agonist action of ATP and FKBP12 bound to RyR1 are required for coupled RyR1 gating. In addition, new pharmacological tools are required to better understand coupled RyR gating. Thus, an additional goal is to identify pharmacological agents that modulate RyR1s in an innovative manner, i.e., help to uncover novel aspects of RyR1 gating and conduction. This investigation suggests that the adenosine based nucleotides, ATP, ADP and AMP, are agonists of RyR1s and promote coupled RyR1 gating in planar lipid bilayers. However, ADP and AMP were unable to maintain coupled RyR1 gating with physiological levels of Mg2+. This suggests that coupled gating would be impaired when the levels ATP decrease, as in muscle fatigue. When ATP was compared to other nucleotides (GTP, ITP, and TTP), the results suggest that the nucleotide agonist action on RyR1s is dependent on the phosphate groups and amino group on the nucleobase. As ATP is the most efficient nucleotide for coupled gating, I also investigated the indirect action of ATP to act as a kinase substrate or alter the cytoskeletal network. The addition of kinases, phosphatases and cytoskeletal modulators did not produce a significant disruption of coupled RyR1 gating. I also tested the role of addition of exogenous FKBP12 to RyR1s that gated independently or had partial coupling, but coupled gating was never improved. Also, the addition of high doses of rapamycin to remove FKBP12 from coupled RyR1 failed to functionally uncouple the channels. Finally, I attempted to find pharmacological agents that could aid in the understanding of coupled RyR1. Some agents were found to modulate RyR1s; however, I did not find a probe that would affect kinetics/conductance of RyR1s and was suitable for comparing coupled gating in bilayers with Ca2+ sparks in cells. Overall, coupled RyR gating is dependent on the physiological modulators ATP and Mg2+. This thesis represents a step forward in identifying the requirements for coupled RyR1 gating and understanding how RyR1s function in cells. Until an understanding of how these receptors communicate in cells is obtained, how different mutations alter the Ca2+ leak will continue to be quite difficult to study.
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Donley, Christopher Blair. "The role of the oestrogen receptor interacting proteins, FKBPL and RBCK1, in breast cancer signalling." Thesis, Queen's University Belfast, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.601364.

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The aim of this thesis was to further characterise the role of FKBPL and RBCKl in the ERa: signalling pathway. Both RBCKl and FKBPL were found to interact with Hsp90 and ER and this interaction was enhanced by E2. Both RBCKl and FKBPL appear [0 be regulated by the oestrogen. However, both FKBPL and RBCKl bind along with ER« to the promoter of pS2, suggesting a potential role for FKBPL and RBCKl in ERa: trans-activation. RBCKl was shown [0 be the ubiquitin ligase for FKBPL. RBCKl was shown to facilitate the attachment of linear chains of ubiquitin to FKBPL. SiRNA knockdown of RBCKl resulted in increased levels of FKBPL in the T47D cell line, but inversely down-regulation of RBCKl in the MCF-7 cell line resulted in a reduction in FKBPL protein levels, suggesting that there is differential regulation of FKBPL by RBCKl depending on the cell line. FKBPL also appears to have a potential role in regulating the self-ubiquitination of RBCK1. RBCKl was also shown to regulate p21 transcription in a mechanism that was independent of p53. RBCKl siRNA knockdown resulted in increased p21 levels but overexpression of RBCKl in the MCF-7 cell line also increased p21 protein levels, suggesting that RBCKl regulates p21 levels through some post-translation modification, possibly through Akt. High levels of FKBPL and RBCKl were independently shown to correlate with increased patient survival in microarray data sets, and a combination of both high RBCKl and FKBPL was the most favourable phenotype. Finally the levels of RBCKl were shown to reduce the efficacy of tamoxifen in the MCF-7 and T47D cell lines, high RBCKl correlated with decreased tamoxifen efficacy. This effect was mirrored in a • micro-array data set, showing high RBCKl predicted worse response for tamoxifen therapy. Therefore RBCKl and FKBPL have potential as novel biomarkers for endocrine therapy.
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Books on the topic "FKBPs"

1

Conference on Neuroimmunophilins (1st 1999 Schlangengad, Germany). Immunophilins in the brain: FKBP Ligands: novel strategies for the treatment of neurodegenerative disorders. Barcelona, Spain: Prous Science, 2000.

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Proyek Pengembangan dan Pemanfaatan Sumber Daya Perikanan Laut (Indonesia), ed. Evaluasi pelaksanaan Forum Koordinasi Pengendalian dan Pengawasan Pemanfaatan Sumber Daya Ikan (FKPPS). Jakarta: Direktorat Bina Sumber Hayati, Direktorat Jenderal Perikanan, Departemen Pertanian, 1995.

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(Editor), B. G. Gold, G. Fischer (Editor), and T. Herdegen (Editor), eds. Immunophilins in the Brain. FKBP Ligands: Novel Strategies for the Treatment of Neurodegenerative Diseases. Prous Science, 2000.

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Book chapters on the topic "FKBPs"

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Klengel, Torsten, and Theo Rein. "FKBP5 Epialleles." In Epigenetics and Neuroendocrinology, 3–21. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-29901-3_1.

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D’Arrigo, Paolo, Martina Tufano, Anna Rea, Simona Romano, and Maria Fiammetta Romano. "FKBP (FK506 Binding Protein)." In Encyclopedia of Signaling Molecules, 1737–67. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101769.

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D’Arrigo, Paolo, Martina Tufano, Anna Rea, Simona Romano, and Maria Fiammetta Romano. "FKBP (FK506 Binding Protein)." In Encyclopedia of Signaling Molecules, 1–31. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101769-1.

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Katoh, Masaru, Giorgio Berton, Anna Baruzzi, Jennifer Boylston, Charles Brenner, Yong-Hun Lee, William Schiemann, et al. "FKBP-Rapamycin-Associated Protein (FRAP)." In Encyclopedia of Signaling Molecules, 623. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100450.

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Lee, Richard S. "Glucocorticoid-Dependent Epigenetic Regulation of Fkbp5." In Epigenetics and Neuroendocrinology, 97–114. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-24493-8_4.

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Cox, Marc B., and David F. Smith. "Functions of the Hsp90-Binding FKBP Immunophilins." In Networking of Chaperones by Co-Chaperones, 13–25. New York, NY: Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-49310-7_2.

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Guy, Naihsuan C., Yenni A. Garcia, Jeffrey C. Sivils, Mario D. Galigniana, and Marc B. Cox. "Functions of the Hsp90-Binding FKBP Immunophilins." In Subcellular Biochemistry, 35–68. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-11731-7_2.

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Ortiz, Nina R., Naihsuan Guy, Yenni A. Garcia, Jeffrey C. Sivils, Mario D. Galigniana, and Marc B. Cox. "Functions of the Hsp90-Binding FKBP Immunophilins." In Subcellular Biochemistry, 41–80. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-14740-1_2.

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Cowling, Rachel J., Paola Vittorioso, Jean-Denis Faure, Michel Caboche, and Catherine Bellini. "The role of PASTICCINO1, an FKBP-like protein, in plant development." In Plant Biotechnology and In Vitro Biology in the 21st Century, 365–68. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4661-6_83.

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Carter*, Guy T. "Chapter 5. Progress in Enhancing the Neurotrophic Effects of Natural FKBP Ligands." In Drug Discovery, 79–95. Cambridge: Royal Society of Chemistry, 2012. http://dx.doi.org/10.1039/9781849734950-00079.

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Conference papers on the topic "FKBPs"

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Faiz, Alen, Dirkje S. Postma, Gerard H. Koppelman, Pieter S. Hiemstra, Peter J. Sterk, Wim Timens, Katrina Steiling, Avrum Spira, Irene H. Heijink, and Maarten van den Berge. "FKBP5 a candidate for corticosteroid insensitivity in COPD." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.oa1779.

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McKeen, H., C. Byrne, P. Jithesh, C. Donley, A. Yakkundi, H. McCarthy, C. Swanton, D. Hirst, and T. Robson. "FKBPL Regulates Estrogen Receptor Signalling and Determines Response to Endocrine Therapy." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-5126.

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Ili, Carmen Gloria, Tamara Viscarra, Juan Carlos Araya, Jaime Lopez, Barbara Mora, Javier Retamal, Susana Aedo, Enrique Bellolio, Juan Carlos Roa, and Priscilla Brebi. "Abstract B28: FKBP6 gene is involved in progression of cervical cancer." In Abstracts: AACR Precision Medicine Series: Cancer Cell Cycle - Tumor Progression and Therapeutic Response; February 28 - March 2, 2016; Orlando, FL. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3125.cellcycle16-b28.

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MacEwan, Melanie E., Ken Wong, Ismatun Swati, Suqing Xie, Mohammad Rasul, Olena Ardacheva, Joseph Buchsbaum, et al. "Abstract 3559: FKBP5 is an androgen-responsive gene in thyroid cancer cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3559.

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Alqudah, A., R. McNally, N. Todd, DJ Grieve, T. Robson, and L. McClements. "4 The role of a novel anti-angiogenic protein, FKBPL, in angiogenesis associated with cardiac dysfunction." In The Scottish Cardiovascular Forum 2018, 3rd February 2018, Trinity Biomedical Science Institute, Trinity College Dublin Ireland. BMJ Publishing Group Ltd and British Cardiovascular Society, 2018. http://dx.doi.org/10.1136/heartjnl-2018-scf.4.

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Faiz, Alen, Marissa Wisman, Pieter S. Hiemstra, Wim Timens, Prescott Woodruff, Stephanie Christenson, Maarten Van Den Berge, Irene H. Heijink, and Gerard H. Koppelman. "Late Breaking Abstract - Functional investigation of the corticosteroid resistance candidate FKBP5 using a CRISPR-Cas9 knockout model." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa372.

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D'Arrigo, Paolo, Michele Russo, Elia Guadagno, Roberto Pacelli, Maria Laura Del Basso De caro, Anna Rea, Martina Tufano, et al. "Abstract 586: Ionizing radiation-induced PD-L1 upregulation in glioma: a crucial role for the molecular chaperone FKBP5." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-586.

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Annett, Stephanie, Gillian Moore, Amy Short, Neermeen Moustafa, Sudipto Das, Darran O'Connor, Cian McCrudden, et al. "Abstract LB-054: FKBPL as a novel therapeutic target and prognostic biomarker in high grade serous ovarian cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-lb-054.

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Hou, Junmei, and Liewei Wang. "Abstract C15: Combined blockade of AKT kinase with gemcitabine overcomes FKBP5-mediated resistance of inhibition of pancreatic tumor growth." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-c15.

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Romano, Simona, Anna Laura Di Pace, Antonio Sorrentino, Giovanna Nappo, Rosanna Martinelli, Rita Bisogni, and Maria Fiammetta Romano. "Abstract 260: FK506 binding protein (FKBP) 51 controls “TNF-related apoptosis inducing ligand” (TRAIL) response in melanoma." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-260.

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Reports on the topic "FKBPs"

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Fan, Beifang, Jianping Ma, Huimin Zhang, Yuhua Liao, Wanxin Wang, Sheng Zhang, Ciyong Lu, and Lan Guo. Association of FKBP5 gene variants with depression susceptibility: a comprehensive meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, August 2020. http://dx.doi.org/10.37766/inplasy2020.8.0086.

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