Relevant bibliographies by topics / FKBP12 protein

Academic literature on the topic 'FKBP12 protein'

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Published: 10 March 2023

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Journal articles on the topic "FKBP12 protein"

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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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ZENG, Baifei, J. Randy MACDONALD, G. James BANN, Konrad BECK, E. Jay GAMBEE, A. Bruce BOSWELL, and Peter Hans BÄCHINGER. "Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis–trans isomerases, is only partially inhibited by FK506." Biochemical Journal 330, no. 1 (February 15, 1998): 109–14. http://dx.doi.org/10.1042/bj3300109.

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The chicken FK506-binding protein FKBP65, a peptidylprolyl cis-trans isomerase, is a rough endoplasmic reticulum protein that contains four domains homologous to FKBP13, another rough endoplasmic reticulum PPIase. Analytical ultracentrifugation suggests that in FKBP65 these four domains are arranged in a linear extended structure with a length of about 26 nm and a diameter of about 3 nm. All four domains are therefore expected to be accessible to substrates. The specificity of FKBP65 towards a number of peptide substrates was determined. The specific activity of FKBP65 is generally lower than that of FKBP12 when expressed as a per domain activity. The substrate specificity of FKBP65 also differs from that of FKBP12. Inhibition studies show that only one of the four domains can be inhibited by FK506, a powerful inhibitor of all other known FKBPs. Furthermore, the same domain seems to be susceptible to inhibition by cyclosporin A. No other FKBPs were shown to be inhibited by cyclosporin A. It is also shown that FKBP65 can catalyse the re-folding of type III collagen in vitro with a kcat/Km = 4.3×103 M-1·s-1.
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Barg, S., J. A. Copello, and S. Fleischer. "Different interactions of cardiac and skeletal muscle ryanodine receptors with FK-506 binding protein isoforms." American Journal of Physiology-Cell Physiology 272, no. 5 (May 1, 1997): C1726—C1733. http://dx.doi.org/10.1152/ajpcell.1997.272.5.c1726.

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In the present study, we compare functional consequences of dissociation and reconstitution of binding proteins FKBP12 and FKBP12.6 with ryanodine receptors from cardiac (RyR2) and skeletal muscle (RyR1). The skeletal muscle RyR1 channel became activated on removal of endogenously bound FKBP12, consistent with previous reports. Both FKBP12 and FKBP12.6 rebind to FKBP-depleted RyR1 and restore its quiescent channel behavior by altering ligand sensitivity, as studied by single-channel recordings in planar lipid bilayers, and macroscopic behavior of the channels (ryanodine binding and net energized Ca2- uptake). By contrast, removal of FKBP12.6 from the cardiac RyR2 did not modulate the function of the channel using the same types of assays as for RyR1. FKBP12 or FKBP12.6 had no effect on channel activity of FKBP12.6-depleted cardiac RyR2, although FKBP12.6 rebinds. Our studies reveal important differences between the two ryanodine receptor isoforms with respect to their functional interaction with FKBP12 and FKBP12.6.
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Chen, Hui, Sourajit M. Mustafi, David M. LeMaster, Zhong Li, Annie Héroux, Hongmin Li, and Griselda Hernández. "Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6." Acta Crystallographica Section D Biological Crystallography 70, no. 3 (February 15, 2014): 636–46. http://dx.doi.org/10.1107/s1399004713032112.

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The primary known physiological function of FKBP12.6 involves its role in regulating the RyR2 isoform of ryanodine receptor Ca2+channels in cardiac muscle, pancreatic β islets and the central nervous system. With only a single previously reported X-ray structure of FKBP12.6, bound to the immunosuppressant rapamycin, structural inferences for this protein have been drawn from the more extensive studies of the homologous FKBP12. X-ray structures at 1.70 and 1.90 Å resolution fromP21andP3121 crystal forms are reported for an unligated cysteine-free variant of FKBP12.6 which exhibit a notable diversity of conformations. In one monomer from theP3121 crystal form, the aromatic ring of Phe59 at the base of the active site is rotated perpendicular to its typical orientation, generating a steric conflict for the immunosuppressant-binding mode. The peptide unit linking Gly89 and Val90 at the tip of the protein-recognition `80s loop' is flipped in theP21crystal form. Unlike the >30 reported FKBP12 structures, the backbone conformation of this loop closely follows that of the first FKBP domain of FKBP51. The NMR resonances for 21 backbone amides of FKBP12.6 are doubled, corresponding to a slow conformational transition centered near the tip of the 80s loop, as recently reported for 31 amides of FKBP12. The comparative absence of doubling for residues along the opposite face of the active-site pocket in FKBP12.6 may in part reflect attenuated structural coupling owing to increased conformational plasticity around the Phe59 ring.
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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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Vervliet, Tim, Jan B. Parys, and Geert Bultynck. "Bcl-2 and FKBP12 bind to IP3 and ryanodine receptors at overlapping sites: the complexity of protein–protein interactions for channel regulation." Biochemical Society Transactions 43, no. 3 (June 1, 2015): 396–404. http://dx.doi.org/10.1042/bst20140298.

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The 12- and 12.6-kDa FK506-binding proteins, FKBP12 (12-kDa FK506-binding protein) and FKBP12.6 (12.6-kDa FK506-binding protein), have been implicated in the binding to and the regulation of ryanodine receptors (RyRs) and inositol 1,4,5-trisphosphate receptors (IP3Rs), both tetrameric intracellular Ca2+-release channels. Whereas the amino acid sequences responsible for FKBP12 binding to RyRs are conserved in IP3Rs, FKBP12 binding to IP3Rs has been questioned and could not be observed in various experimental models. Nevertheless, conservation of these residues in the different IP3R isoforms and during evolution suggested that they could harbour an important regulatory site critical for IP3R-channel function. Recently, it has become clear that in IP3Rs, this site was targeted by B-cell lymphoma 2 (Bcl-2) via its Bcl-2 homology (BH)4 domain, thereby dampening IP3R-mediated Ca2+ flux and preventing pro-apoptotic Ca2+ signalling. Furthermore, vice versa, the presence of the corresponding site in RyRs implied that Bcl-2 proteins could associate with and regulate RyR channels. Recently, the existence of endogenous RyR–Bcl-2 complexes has been identified in primary hippocampal neurons. Like for IP3Rs, binding of Bcl-2 to RyRs also involved its BH4 domain and suppressed RyR-mediated Ca2+ release. We therefore propose that the originally identified FKBP12-binding site in IP3Rs is a region critical for controlling IP3R-mediated Ca2+ flux by recruiting Bcl-2 rather than FKBP12. Although we hypothesize that anti-apoptotic Bcl-2 proteins, but not FKBP12, are the main physiological inhibitors of IP3Rs, we cannot exclude that Bcl-2 could help engaging FKBP12 (or other FKBP isoforms) to the IP3R, potentially via calcineurin.
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Ozawa, Terutaka. "Effects of FK506 on Ca2+ Release Channels (Review)." Perspectives in Medicinal Chemistry 2 (January 2008): PMC.S382. http://dx.doi.org/10.4137/pmc.s382.

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Tacrolimus (FK506), which was isolated from the fermentation broth of Streptomyces tsukubaensis No. 9993, has an immunosuppressive effect. In T-lymphocytes, FK506 binds to the intracellular receptor, a 12-kDa FK506-binding protein (FKBP12). The FK506-FKBP12 complex binds to the phosphatase calcineurin (CN) and inhibits the activity of CN. By inhibition of the activity of CN, dephosphorylation of a nuclear factor of activated T-cells (NFAT) is inhibited, and translocation of the NFAT to the nucleus is suppressed. Thereby, the production of T-cell-derived mediators such as interleukin 2 (IL-2) is inhibited, and the proliferation of cytotoxic T-cells is suppressed. In muscle cells, FKBP12 and FKBP12.6 are associated with ryanodine-sensitive Ca2+ release channels (ryanodine receptors: RyRs) on the skeletal and cardiac muscle sarcoplasmic reticulum (SR), respectively. FK506 modulates the RyR by dissociating FKBP12 or FKBP12.6 from the RyR complex. FKBP12 is also associated with inositol 1,4,5-trisphosphate (IP3)-sensitive Ca2+ release channels (IP3 receptors: IP3Rs) on the endoplasmic reticulum (ER) of non-muscle cells. The IP3R-FKBP12 complex binds to CN, which dephosphorylates the protein kinase C (PKC) phosphorylation site on the receptor. When FKBP12 is dissociated from the IP3R complex by FK506, CN is also dissociated from the IP3R. Thereby, the IP3R is phosphorylated by PKC, and the receptor is modulated. Recently, it was found that FK506 itself induces Ca2+ release through RyRs in some tissues.
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Dolinski, Kara J., and Joseph Heitman. "Hmo1p, a High Mobility Group 1/2 Homolog, Genetically and Physically Interacts With the Yeast FKBP12 Prolyl Isomerase." Genetics 151, no. 3 (March 1, 1999): 935–44. http://dx.doi.org/10.1093/genetics/151.3.935.

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Abstract The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. FKBP12 is a ubiquitous, highly conserved, abundant enzyme that catalyzes a rate-limiting step in protein folding: peptidyl-prolyl cis-trans isomerization. However, FKBP12 is dispensible for viability in both yeast and mice, and therefore does not play an essential role in protein folding. The functions of FKBP12 may involve interactions with a number of partner proteins, and a few proteins that interact with FKBP12 in the absence of FK506 or rapamycin have been identified, including the ryanodine receptor, aspartokinase, and the type II TGF-β receptor; however, none of these are conserved from yeast to humans. To identify other targets and functions of FKBP12, we have screened for mutations that are synthetically lethal with an FKBP12 mutation in yeast. We find that mutations in HMO1, which encodes a high mobility group 1/2 homolog, are synthetically lethal with mutations in the yeast FPR1 gene encoding FKBP12. Δhmo1 and Δfpr1 mutants share two phenotypes: an increased rate of plasmid loss and slow growth. In addition, Hmo1p and FKBP12 physically interact in FKBP12 affinity chromatography experiments, and two-hybrid experiments suggest that FKBP12 regulates Hmo1p-Hmo1p or Hmo1p-DNA interactions. Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions.
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Tang, Wang-Xian, Ya-Fei Chen, Ai-Ping Zou, William B. Campbell, and Pin-Lan Li. "Role of FKBP12.6 in cADPR-induced activation of reconstituted ryanodine receptors from arterial smooth muscle." American Journal of Physiology-Heart and Circulatory Physiology 282, no. 4 (April 1, 2002): H1304—H1310. http://dx.doi.org/10.1152/ajpheart.00843.2001.

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cADP ribose (cADPR) serves as second messenger to activate the ryanodine receptors (RyRs) of the sarcoplasmic reticulum (SR) and mobilize intracellular Ca2+in vascular smooth muscle cells. However, the mechanisms mediating the effect of cADPR remain unknown. The present study was designed to determine whether FK-506 binding protein 12.6 (FKBP12.6), an accessory protein of the RyRs, plays a role in cADPR-induced activation of the RyRs. A 12.6-kDa protein was detected in bovine coronary arterial smooth muscle (BCASM) and cultured CASM cells by being immunoblotted with an antibody against FKBP12, which also reacted with FKBP12.6. With the use of planar lipid bilayer clamping techniques, FK-506 (0.01–10 μM) significantly increased the open probability ( NP O) of reconstituted RyR/Ca2+release channels from the SR of CASM. This FK-506-induced activation of RyR/Ca2+ release channels was abolished by pretreatment with anti-FKBP12 antibody. The RyRs activator cADPR (0.1–10 μM) markedly increased the activity of RyR/Ca2+ release channels. In the presence of FK-506, cADPR did not further increase the NP O of RyR/Ca2+ release channels. Addition of anti-FKBP12 antibody also completely blocked cADPR-induced activation of these channels, and removal of FKBP12.6 by preincubation with FK-506 and subsequent gradient centrifugation abolished cADPR-induced increase in the NP O of RyR/Ca2+ release channels. We conclude that FKBP12.6 plays a critical role in mediating cADPR-induced activation of RyR/Ca2+ release channels from the SR of BCASM.
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Reiken, Steven, Alain Lacampagne, Hua Zhou, Aftab Kherani, Stephan E. Lehnart, Chris Ward, Fannie Huang, et al. "PKA phosphorylation activates the calcium release channel (ryanodine receptor) in skeletal muscle." Journal of Cell Biology 160, no. 6 (March 10, 2003): 919–28. http://dx.doi.org/10.1083/jcb.200211012.

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The type 1 ryanodine receptor (RyR1) on the sarcoplasmic reticulum (SR) is the major calcium (Ca2+) release channel required for skeletal muscle excitation–contraction (EC) coupling. RyR1 function is modulated by proteins that bind to its large cytoplasmic scaffold domain, including the FK506 binding protein (FKBP12) and PKA. PKA is activated during sympathetic nervous system (SNS) stimulation. We show that PKA phosphorylation of RyR1 at Ser2843 activates the channel by releasing FKBP12. When FKB12 is bound to RyR1, it inhibits the channel by stabilizing its closed state. RyR1 in skeletal muscle from animals with heart failure (HF), a chronic hyperadrenergic state, were PKA hyperphosphorylated, depleted of FKBP12, and exhibited increased activity, suggesting that the channels are “leaky.” RyR1 PKA hyperphosphorylation correlated with impaired SR Ca2+ release and early fatigue in HF skeletal muscle. These findings identify a novel mechanism that regulates RyR1 function via PKA phosphorylation in response to SNS stimulation. PKA hyperphosphorylation of RyR1 may contribute to impaired skeletal muscle function in HF, suggesting that a generalized EC coupling myopathy may play a role in HF.
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Dissertations / Theses on the topic "FKBP12 protein"

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Blackburn, Elizabeth Anne. "Biophysical studies of protein-ligand interactions and the discovery of FKBP12 inhibitors." Thesis, University of Edinburgh, 2010. http://hdl.handle.net/1842/6504.

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The principal aim of this study was to discover, through virtual screening, new nonimmunosuppressive inhibitors for the human immunophilin FKBP12, a target of the immunosuppressant drugs rapamycin and FK506. The enzyme acts as peptidyl-prolyl isomerase catalysing protein folding in the cell. Structurally similar isomerase domains are important for molecular recognition in multi-domain chaperone proteins. FKBP inhibitors have been shown to have protective effects against nerve damage and are therefore interesting targets for the treatment of neurodegenerative diseases. Virtual screening has been used to discover novel inhibitors for protein drug targets. Recent advances in computational power and the availability of large virtual libraries, such as the EDULISS database at Edinburgh University, have enhanced the appeal of this approach. X-ray structures of known protein-ligand complexes were examined to obtain an understanding of the key non-covalent interactions in the FKBP12 binding pocket. Virtual screening hits were selected using macromolecular docking and programs that employed a ligand-based approach. The bulk of the virtual screening in this study used Edinburgh University’s in-house program LIDAEUS. In the course of this study nearly three hundred compounds were screened in the laboratory using biophysical and biochemical binding assays. Thirty four compounds were found to have an affinity for FKBP12 of less than one hundred micromolar. To test virtual hits, it was necessary to select the most appropriate medium-throughput biophysical assay. The aim was to employ methods with sufficient sensitivity to detect compounds with affinity in the order of one hundred micromolar, coupled with the capacity to screen hundreds of compounds in a week. This study used a wide variety of biophysical techniques, these including: electrospray ionisation mass spectrometry, surface plasmon resonance and isothermal titration calorimetry. There was a particular emphasis on the quality of data from electrospray ionisation mass spectrometry. A correlation was found between the cone voltages that gave 50 % dissociation of the complex with the enthalpic contribution to the free energy of binding. From the careful examination of the differences in charge-state distributions between a pure protein and a protein-ligand mixture, it was possible to determine if a protein-ligand complex had been present in solution prior to dissociation during the electrospray process. This observation provides the basis for an assay that could be of general utility in detecting very weak inhibitors.
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Zibrova, Darya. "Adenovirus-mediated gene transfer of FK506-binding proteins FKBP12.6 and FKBP12 in failing and non-failing rabbit ventricular myocytes." Doctoral thesis, [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972602275.

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Main, Ewan Ralph Gibson. "Studies on the immunosuppressant binding protein FKBP12 and the nuclear/steroid receptors vitamin D3 and oestrogen." Thesis, University of Cambridge, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621749.

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Chaurasia, S. "IN SILICO STUDY OF PROTEIN PROTEIN INTERACTION STABILIZATION AND MECHANICAL FORCE APPLICATION ON BIOMOLECULES." Doctoral thesis, Università degli Studi di Milano, 2014. http://hdl.handle.net/2434/229253.

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Targeting protein-protein interactions is a challenging task in drug discovery process. Despite the challenges, several studies have provided evidences for the development of small molecules modulating protein-protein interactions. In Part I, it is demonstrated that how a small molecule can induce the formation of an otherwise unstable protein-protein complex. A study of the stabilization of a FKBP12-FRB complex by a small molecule rapamycin is presented. The stability of the complex is analyzed and its interactions are characterized at the atomic level by performing free energy calculations and computational alanine scanning. It is shown that rapamycin stabilizes the complex by acting as a bridge between the two proteins; and the complex is stable only in the presence of rapamycin. The reported results and the good performance of standard molecular modeling techniques in describing the model system can be interesting not only in the design and development of improved molecules acting as FKBP12–FRB protein interaction stabilizers, but also in the somehow neglected study of protein-protein interactions stabilizers in general. In Part II, studies regarding computational modeling of the application of mechanical force to biomolecules is presented. This part is further divided into two chapters since the investigations have been performed on two biological systems. In the first chapter of Part II (chapter 6), it is described that how the osmolyte molecules affect the mechanical unfolding of a peptide. The mechanical unfolding of peptide has been performed by using Steered Molecular Dynamics. In this study, the effect of four different osmolytes on the free energy difference between the folded and the denatured state have been calculated. The observed trend mirrors the expected behavior of the studied osmolytes and unfolding pathways analysis allows an insight into the mechanism of action of osmolytes. After the successful application of Steered molecular dynamics technique on the β-hairpin peptide, the same is applied on tubulin heterodimers for the in-depth study of the lateral and longitudinal interactions which are responsible for the stability and dynamics of the microtubules. In the other chapter of Part II (chapter 7), these interactions are studied with the help of mechanical dissociation of the tubulin heterodimers. These studies have allowed the identification of the critical interactions responsible for the binding of tubulin heterodimers laterally as well as longitudinally. The observations obtained could be important for the design of compounds that target these interactions and acts as microtubule inhibitors or stabilizers.
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Kim, Ju Young. "M1 muscarinic acetylcholine receptor regulation of endogenous transient receptor potential-canonical, subtype 6 (TRPC6) channels." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1117570788.

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Thesis (Ph. D.)--Ohio State University, 2005.
Title from first page of PDF file. Document formatted into pages; contains xviii, 178 p.; also includes graphics. Includes bibliographical references (p. 163-178). Available online via OhioLINK's ETD Center
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De, Cicco Maristella Verfasser], Sonja A. [Akademischer Betreuer] [Gutachter] Dames, and Aymelt [Gutachter] [Itzen. "NMR characterization of the membrane-localized interaction network between the kinase TOR, the GTPase Rheb and the FKBP12-like protein FKBP38. / Maristella De Cicco ; Gutachter: Aymelt Itzen, Sonja A. Dames ; Betreuer: Sonja A. Dames." München : Universitätsbibliothek der TU München, 2017. http://d-nb.info/1147566178/34.

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Davies, Todd Howard. "Regulation of Glucocorticoid Receptor Function by TPR-domain Proteins." University of Toledo Health Science Campus / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=mco1098292002.

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Olivieri, Lilian. "Recherche et caractérisation par dynamique moléculaire d'états intermédiaires pour la complexation entre la protéine FKBP12 et des ligands de haute affinité." Thesis, La Réunion, 2012. http://www.theses.fr/2012LARE0011/document.

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FKBP12 est une protéine ubiquitaire, principalement cytosolique, qui est au carrefour de plusieurs voies signalétiques. Son abondance naturelle dans les tissus nerveux peut être reliée à son implication dans les maladies neurodégénératives telles que les maladies d'Alzheimer et de Parkinson ainsi que dans les neuropathies périphériques et diabétiques ou dans des blessures des cordons spinaux. De nombreuses études ont montré que des molécules exogènes (ligands) venant se fixer sur cette protéine permettent la régénération d'un grand nombre de connexions neuronales endommagées. Une difficulté provient cependant du fait que, pour un ligand donné, il n'existe aucune relation claire entre sa structure et sa capacité de liaison à FKBP12. Notre étude vise ainsi à rationaliser la relation entre la structure d'un ligand et son affinité pour cette protéine. Deux complexes modèles, formés entre FKBP12 et chacun des deux ligands 8 et 308, ont été utilisés. Ces deux ligands de haute affinité ont des structures différentes. Notre travail s'est appuyé sur des simulations de dynamique moléculaire pour caractériser l'état intermédiaire qui est formé transitoirement lors du processus de complexation entre la protéine et son ligand. Dans cet état particulier, l'identification des interactions naissantes entre les partenaires a permis (i) de comprendre l'implication des différentes parties du ligand dans le mécanisme de reconnaissance avec FKBP12 et (ii) de rationaliser les affinités de certains ligands apparentés
FKBP12 is an ubiquitous, mostly cytosolic, protein found at the crossroads of several signaling pathways. Its natural abundance in the nervous tissues can be related to its implication in neurodegenerative diseases like Alzheimer's and Parkinson's as well as in peripheral neuropathies and diabetes or in injuries of the spinal cords. Several studies have demonstrated that exogenous molecules (ligands) that can bind to FKBP12 allow the regeneration of many damaged neuron connections. However, there is no clear relationship between the structure of a ligand and its ability to bind to FKBP12. Our study aims at rationalizing the relationship between the structure of a ligand and its affinity to FKBP12. Two model complexes, formed between FKBP12 and each of the two high-affinity ligands 8 and 308, were studied. These two ligands are structurally different. We used molecular dynamics simulations to characterize the intermediate state that is transiently formed during the binding process between the protein and its ligand. In this state, the analysis of the nascent interactions allowed (i) to unravel the role played by the various ligand moieties in the recognition process with FKBP12 and (ii) to rationalize the affinities of related ligands
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Belnou, Mathilde. "Études biophysiques des propriétés et des interactions entre trois protéines impliquées dans la maladie d’Alzheimer : récepteur des oestrogènes α, Calmoduline et FKBP52." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066262.

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Nous nous sommes intéressés à plusieurs protéines impliquées dans la maladie d’Alzheimer, notamment la protéine FKBP52, la calmoduline et le ROα. Nous nous sommes attachés à apporter quelques éléments de réponse quant à la formation d'un éventuel hétérocomplexe ROα/Ca4CaM/FKBP52. Dans une première partie, nous avons voulu étudier quelques bases moléculaires de l'interaction entre FKBP52 et la Ca4CaM, afin de mieux comprendre la pertinence biologique de cette affinité. Après avoir produit différents domaines de la protéine FKBP52 et la Ca4CaM, différentes techniques d’interaction protéine/protéine ont été utilisées. L'approche protéique de ce travail a été confortée par une approche peptidique. Elles ont permis de cibler le troisième domaine comme lieu de l’interaction. Pour la première fois, il a été totalement attribué par RMN et les sites concernés par l’interaction ont pu être discriminés. Par ailleurs, il a été montré que le premier domaine de FKBP52 pouvait interagir intermoléculairement avec ROα, par un motif en coude β de type II. Le ROα est un facteur de transcription dont l'activité dépend d'un certain nombre de coactivateurs parmi lesquels Ca4CaM. Le peptide issu de la séquence de recrutement de la calmoduline au sein du ROα (séquence 298-310) a fait l’objet au sein du groupe de nombreuses publications. Il a été montré que ce peptide possédait un caractère amyloïde. Bien qu’il n’existe aucun lien apparent entre cette caractéristique et une quelconque pathologie associée, la cinétique de formation des fibres issues de ce peptide dans différentes conditions de pH et de concentrations a été étudiée
We are interested in several proteins involved in the Alzheimer disease, in particular the FKBP52, calmodulin and ERα. We have provided some answers concerning the formation of a possible ROα/Ca4CaM/FKBP52 heterocomplex. In a first part, we wanted to study the molecular basis of the interaction between FKBP52 and Ca4CaM, to better understand the biological relevance of this affinity. After producing different domains of the FKBP52 protein and Ca4CaM, various techniques such as ITC, SPR, fluorescence or NMR were used. The protein approach of this work was supported by a peptide based study. These approaches have made it possible to target the third domain as the place of interaction. For the first time, the TPR domain was assigned by NMR spectroscopy and the sequences involved in the interaction could be discriminated. Furthermore, it was shown that the first domain of FKBP52 could interact intermolecularly with the ROα, by a type II β-turn motif. ROα is a transcription factor whose activity depends on a number of coactivators including Ca4CaM. The peptide resulting from the recruitment sequence of calmodulin within ROα (sequence 298-310) has been the subject of numerous publications within the group. It has been shown that this peptide has an amyloid character. Although there is no apparent link between this feature and any associated pathology, the kinetics of fiber formation from this peptide under different pH and concentration conditions has been studied
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Stechschulte, Lance A. "The Co-chaperones FKBP51 and PP5 Control Nuclear Receptor Phosphorylation and Adipogenesis." University of Toledo Health Science Campus / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=mco1370871316.

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Book chapters on the topic "FKBP12 protein"

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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, Mark Handley, Marga Gual-Soler, Tomohiko Taguchi, Jennifer L. Stow, et al. "Rapamycin and FKBP12 Target-1 Protein (RAFT1)." In Encyclopedia of Signaling Molecules, 1596. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101146.

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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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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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"Rapamycin and FKBP12 Target-1 Protein (RAFT1)." In Encyclopedia of Signaling Molecules, 4462. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103220.

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Krakow, Deborah, and Yasemin Alanay. "FKBP10 (FKBP65 Protein), Osteogenesis Imperfecta and Bruck Syndrome." In Osteogenesis Imperfecta, 151–57. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-397165-4.00015-0.

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"FKBP-Rapamycin-Associated Protein (FRAP)." In Encyclopedia of Signaling Molecules, 1767. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101274.

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Buchner, Johannes, Tina Weikl, Hans Bügl, Franziska Pirkl, and Suchira Bose. "[33] Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52." In Methods in Enzymology, 418–29. Elsevier, 1998. http://dx.doi.org/10.1016/s0076-6879(98)90035-0.

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Conference papers on the topic "FKBP12 protein"

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Ioris, R. Maciel. "PO-108 FKBP10 is an oncofetal protein that supports lung cancer growth by promoting protein translation elongation." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.149.

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Komaragiri, Shravan Kumar. "Abstract 3061: Role of ID4 (inhibitor of DNA binding protein 4) in FKBP52-AR pathway." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3061.

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Komaragiri, Shravan Kumar. "Abstract 3061: Role of ID4 (inhibitor of DNA binding protein 4) in FKBP52-AR pathway." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3061.

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Ratz, Veronika, Anne-Christine Plank, Anja Schulze-Krebs, and Stephan von Hörsten. "A13 Expression of FKBP51 and HAP40 protein in a congenic rat model of huntington disease." In EHDN 2018 Plenary Meeting, Vienna, Austria, Programme and Abstracts. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/jnnp-2018-ehdn.13.

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Romano, Simona, Antonio Sorrentino, AnnaLaura Di Pace, Stefania Staibano, Massimo Mascolo, Rita Bisogni, Gennaro Ilardi, and Maria Fiammetta Romano. "Abstract 4999: FK506 binding protein 51 (FKBP51) sustains stemness and the metastatic potential of malignant melanoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4999.

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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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Storer, CL, K. Olivares, RJ Fletterick, P. Webb, and MB Cox. "Abstract P5-07-02: Analysis of a novel synergistic relationship between the FK506 binding protein FKBP52 and beta catenin in androgen receptor signaling pathways." In Abstracts: Thirty-Fifth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 4‐8, 2012; San Antonio, TX. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/0008-5472.sabcs12-p5-07-02.

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Mroz, Robert M., Adam Holownia, Elzbieta Chyczewska, and Jan J. Braszko. "Heat Shock Proteins And FKBP51 Expression In Sputum Cells Of COPD Patients During Formoterol/Corticosteroid/Theophylline Therapy." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4476.

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Romano, Simona, Giovanna Nappo, Elena Cesaro, Antonio Candela, and Maria Fiammetta Romano. "Abstract 755: FK506 binding protein 51 (FKBP51) binds to p300 and acts as transcriptional co-regulator of ABCG2 gene expression in melanoma." 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.am2013-755.

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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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