Relevant bibliographies by topics / Immunophilins

Academic literature on the topic 'Immunophilins'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Immunophilins"

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De Leo, Sonia A., Nadia R. Zgajnar, Gisela I. Mazaira, Alejandra G. Erlejman, and Mario D. Galigniana. "Role of the Hsp90-Immunophilin Heterocomplex in Cancer Biology." Current Cancer Therapy Reviews 16, no. 1 (February 6, 2020): 19–28. http://dx.doi.org/10.2174/1573394715666190102120801.

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The identification of new factors that may function as cancer markers and become eventual pharmacologic targets is a challenge that may influence the management of tumor development and management. Recent discoveries connecting Hsp90-binding immunophilins with the regulation of signalling events that can modulate cancer progression transform this family of proteins in potential unconventional factors that may impact on the screening and diagnosis of malignant diseases. Immunophilins are molecular chaperones that group a family of intracellular receptors for immunosuppressive compounds. A subfamily of the immunophilin family is characterized by showing structural tetratricopeptide repeats, protein domains that are able to interact with the C-terminal end of the molecular chaperone Hsp90, and via the proper Hsp90-immunophilin complex, the biological properties of a number of client-proteins involved in cancer biology are modulated. Recent discoveries have demonstrated that two of the most studied members of this Hsp90- binding subfamily of immunophilins, FKBP51 and FKBP52, participate in several cellular processes such as apoptosis, carcinogenesis progression, and chemoresistance. While the expression levels of some members of the immunophilin family are affected in both cancer cell lines and human cancer tissues compared to normal samples, novel regulatory mechanisms have emerged during the last few years for several client-factors of immunophilins that are major players in cancer development and progression, among them steroid receptors, the transctiption factor NF-κB and the catalytic subunit of telomerase, hTERT. In this review, recent findings related to the biological properties of both iconic Hsp90-binding immunophilins, FKBP51 and FKBP52, are reviewed within the context of their interactions with those chaperoned client-factors. The potential roles of both immunophilins as potential cancer biomarkers and non-conventional pharmacologic targets for cancer treatment are discussed.
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Marks, A. R. "Cellular functions of immunophilins." Physiological Reviews 76, no. 3 (July 1, 1996): 631–49. http://dx.doi.org/10.1152/physrev.1996.76.3.631.

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Immunophilins are members of a highly conserved family of proteins all of which are cis-trans peptidyl-prolyl isomerases. The prototypic members of the immunophilin family, cyclophilin A and FKPB12, were discovered on the basis of their ability to bind and mediate the immunosuppressive effects of the drugs cyclosporin, FK506, and rapamycin. However, the prolyl isomerase activity of these proteins is not involved in any of the immunosuppressive effects. Indeed, despite the fact that all members of the family are prolyl isomerases, the cellular role of this enzymatic function has not been clearly defined. In many cases, immunophilins are widely expressed and are present at high levels in some tissues. Moreover, while the number of proteins that belong to the immunophilin family continues to grow, the natural cellular functions of all but a few remain obscure. An example where immunophilins do appear to have a defined cellular role, in the absence of immunosuppressive ligands, is the modulation of intracellular calcium release channel function by FKBP12 and FKBP12.6. In this case, FKBPs are integral parts of three types of calcium release channel complexes, skeletal and cardiac ryanodine receptors and the inositol 1,4,5-trisphosphate receptor. In each case, FKBPs modulate channel function possibly by enhancing the cooperativity between subunits.
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Schreiber, Stuart L., Jun Lui, Mark W. Albers, Michael K. Rosen, Robert F. Standaert, Thomas J. Wandless, and Patricia K. Somers. "Molecular Recognition of Immunophilins and Immunophilin-Ligand Complexes." Tetrahedron 48, no. 13 (March 1992): 2545–58. http://dx.doi.org/10.1016/s0040-4020(01)88520-3.

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Tomašić Paić, Ana, and Hrvoje Fulgosi. "Chloroplast immunophilins." Protoplasma 253, no. 2 (May 12, 2015): 249–58. http://dx.doi.org/10.1007/s00709-015-0828-z.

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Wiederrecht, Greg, and Felicia Etzkorn. "The immunophilins." Perspectives in Drug Discovery and Design 2, no. 1 (August 1994): 57–84. http://dx.doi.org/10.1007/bf02171737.

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Mesa, Annia, Jason A. Somarelli, and Rene J. Herrera. "Spliceosomal immunophilins." FEBS Letters 582, no. 16 (June 9, 2008): 2345–51. http://dx.doi.org/10.1016/j.febslet.2008.06.006.

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Nair, S. C., R. A. Rimerman, E. J. Toran, S. Chen, V. Prapapanich, R. N. Butts, and D. F. Smith. "Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor." Molecular and Cellular Biology 17, no. 2 (February 1997): 594–603. http://dx.doi.org/10.1128/mcb.17.2.594.

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A cDNA for human FKBP51 has been cloned and sequenced, and protein products have been expressed in both in vitro and bacterial systems. The deduced amino acid sequence for human FKBP51 is 90% identical to sequences of recently described murine proteins and is 55% identical to the sequence of human FKBP52. Human FKBP51 mRNA is expressed in a wide range of tissues, and the protein has peptidylprolyl isomerase activity that is inhibited by FK506 but not cyclosporine. FKBP51 is the same as a previously described progesterone receptor-associated immunophilin that, similar to FKBP52 and cyclophilin 40, is an Hsp90-binding protein and appears in functionally mature steroid receptor complexes along with Hsp90 and p23. Each of the three receptor-associated immunophilins displays interactions with progesterone receptor that are more dynamic than Hsp90-receptor interactions. Whereas FKBP52 and FKBP51 compete about equally well for binding to Hsp90 in a purified system, FKBP51 accumulates preferentially in progesterone receptor complexes assembled in a cell-free system. This observation provides a precedent for differential interactions between Hsp90-associated immunophilins and target proteins such as steroid receptors.
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Norville, Isobel H., Katherine O'Shea, Mitali Sarkar-Tyson, Suxin Zheng, Richard W. Titball, Gabriele Varani, and Nicholas J. Harmer. "The structure of a Burkholderia pseudomallei immunophilin–inhibitor complex reveals new approaches to antimicrobial development." Biochemical Journal 437, no. 3 (July 13, 2011): 413–22. http://dx.doi.org/10.1042/bj20110345.

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Mips (macrophage infectivity potentiators) are a subset of immunophilins associated with virulence in a range of micro-organisms. These proteins possess peptidylprolyl isomerase activity and are inhibited by drugs including rapamycin and tacrolimus. We determined the structure of the Mip homologue [BpML1 (Burkholderia pseudomallei Mip-like protein 1)] from the human pathogen and biowarfare threat B. pseudomallei by NMR and X-ray crystallography. The crystal structure suggests that key catalytic residues in the BpML1 active site have unexpected conformational flexibility consistent with a role in catalysis. The structure further revealed BpML1 binding to a helical peptide, in a manner resembling the physiological interaction of human TGFβRI (transforming growth factor β receptor I) with the human immunophilin FKBP12 (FK506-binding protein 12). Furthermore, the structure of BpML1 bound to the class inhibitor cycloheximide N-ethylethanoate showed that this inhibitor mimics such a helical peptide, in contrast with the extended prolyl-peptide mimicking shown by inhibitors such as tacrolimus. We suggest that Mips, and potentially other bacterial immunophilins, participate in protein–protein interactions in addition to their peptidylprolyl isomerase activity, and that some roles of Mip proteins in virulence are independent of their peptidylprolyl isomerase activity.
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Hamilton, G. S., and J. P. Steiner. "Immunophilins: Beyond Immunosuppression." Journal of Medicinal Chemistry 41, no. 26 (December 1998): 5119–43. http://dx.doi.org/10.1021/jm980307x.

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Zgajnar, Nadia, Sonia De Leo, Cecilia Lotufo, Alejandra Erlejman, Graciela Piwien-Pilipuk, and Mario Galigniana. "Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52." Biomolecules 9, no. 2 (February 1, 2019): 52. http://dx.doi.org/10.3390/biom9020052.

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Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects.
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Dissertations / Theses on the topic "Immunophilins"

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Dornan, Jacqueline. "Immunophilins : an investigation into function and structure." Thesis, University of Edinburgh, 2001. http://hdl.handle.net/1842/22159.

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The work described in this thesis focused on the over-expression, purification, biochemical characterisation, crystallisation and 3-D structure determination of three members of the immunophilin family. The overall goal of the project was to use biochemical and structural information derived from these studies to assist in the elucidation of the various roles played by these proteins in diverse systems. Cycophilin 3. Cloning and expression of eleven cyclophilin homologues from the free-living nematode Caenorhabditis elegans (C. elegans) has recently been reported. Cyclophilin 3 (Cyc-3), one of the most abundantly expressed isoforms, was chosen as the initial target for further study. The structure of the protein was solved to high resolution, allowing identification of a number of key structural features that differ from those of the archetypal cyclophilin, Cyclophilin A. These newly determined features, which may prove to be functionally significant, were used to define a new cyclophilin subfamily. Cycophilin 40. Cyclophilin 40 (Cyp 40) is a two domain immunophilin containing a conserved cyclophilin domain linked via a charged linker region to the C-terminal domain comprised largely of three copies of the tetratricopeptide repeat (TPR) motif. Cyp 40 constitutes part of the “mature” steroid hormone receptor complex, interactions with Hsp90 have been described, although the exact nature of the interaction has not been well defined. Using cloned bovine Cyp 40, two very different crystal forms were grown. FKBP22. Isolation of FKBP22 for the endoplasmic reticulum of Neurosporra crassa (N. crassa) has recently been reported. The C-terminal sequence appears to be unique among other FKBP sequences, being rather highly charged and is consistent with an amphipathic helical conformation. Crystallisation and preliminary partial X-ray structure determination of FKBP22 from N. crassa are reported.
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Morgan, Gloria Yvonne. "The expression of immunophilins in cells and organelles." Thesis, University of Sussex, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282145.

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McKenzie, Neil Iain. "The immunophilins as drug targets : development of novel fluorescence assays." Thesis, University of Edinburgh, 2014. http://hdl.handle.net/1842/17961.

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The immunophilins are a superfamily of proteins comprising the cyclophilins, the FKBPs and the parvulin sub-families. Members are present ubiquitously in plant and animal cells, acting as both prolyl-isomerases and signalling proteins. Some also have chaperone activity. The prolyl isomerase function of the immunophilins has been identified as being central to progression of a large number of diseases, making them tempting drug targets. Whilst there are several assays which can be used to identify inhibitors of the prolyl isomerase function, they are hampered by one or more problems: multistep mechanisms, poor signal-to-noise ratios, expensive, laborious and unamenable to high throughput screening. Multiple fluorescent systems (fluorescence anisotropy, FRET, 2D-FIDA/FCS) and several technologies (solution and solid phase synthesis, solution and solid phase screening, combinatorial synthesis, and stopped-flow spectrometry) were explored to develop a system suitable for fast, efficient screening of immunophilins. The most promising of these is a prototype assay based on the design, cloning, expression and production of fluorescently labelled mutant of cyclophilin B, which shows an increase in fluorescence emission upon cyclosporin ligand binding.
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McCann, Fiona Elizabeth. "Studies on novel immunophilins and the effects of immunosuppressant drugs on neurons." Thesis, University of Kent, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.246593.

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Davies, Todd Howard. "Regulation of glucocorticoid receptor function by associated TPR-domain proteins." Connect to full-text via OhioLINK ETD Center, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1098292002.

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Thesis (Ph. D.)--Medical College of Ohio, 2003.
"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Medical Sciences." Major advisor: Edwin Sanchez. Includes abstract. Document formatted into pages: iv, 126 p. Title from title page of PDF document. Includes bibliographical references (p. 100-124).
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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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Cluning, Carmel. "Steroid receptor-associated immunophilins : influence of targeted knockdown and altered expression on receptor signalling." University of Western Australia. School of Medicine and Pharmacology, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0215.

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[Truncated abstract] Steroid receptors belong to the superfamily of nuclear receptors, and include the androgen receptor (AR), estrogen receptors (ER[alpha] and ER[beta], glucocorticoid receptor (GR), mineralocorticoid receptor (MR), and the progesterone receptors (PRA and PRB). Before binding ligand, the receptor undergoes biochemical and structural modifications through a series of interactions with molecular chaperones and cochaperones all within a receptor heterocomplex. The mature receptor complexes with the major chaperone Hsp90, the stabilising cochaperone p23, and one member of a group of cochaperones termed immunophilins. Steroid receptor-associated immunophilins include the cyclophilin, CyP40, two FK506-binding proteins, FKBP51 and FKBP52, and the protein phosphatase, PP5. Immunophilins are characterised by the presence of TPR domains which compete directly for the TPR-acceptor site within Hsp90. This leads to mutually exclusive, immunophilin-containing receptor complexes. While PP5 contains a C-terminal phosphatase domain, CyP40, FKBP51 and FKBP52 each contain an N-terminal peptidyl prolyl isomerase (PPIase) domain, which catalyses the cis/trans isomerisation of prolyl peptide bonds. FKBP52 has been demonstrated to potentiate the ligand-dependent activity of AR, GR and PR, but not ER[alpha]. Knowing that CyP40 is the preferred immunophilin associated with the ER[alpha] heterocomplex, it was hypothesised that this immunophilin plays a role in ER[alpha] function. ... As all mutants maintained this potentiating activity it was concluded that the five altered residues found within gpGR do not contribute to the altered interaction of FKBP52 and receptor. However, it cannot be discounted that FKBP51 is more competitive for gpGR. Immunophilins are hormonally regulated, with FKBP52 found to be essential for female fertility in mice. It was hypothesised that levels of immunophilins, associated with steroid receptors important in the menstrual cycle, would be regulated to reflect hormonal activity within cycling endometrium. Human pre-menopausal endometrial sections taken from different phases of the menstrual cycle were examined immunohistochemically for expression of CyP40, FKBP51, FKBP51 and PP5. Immunophilin levels peaked at the mid-secretory phase correlating with stromal decidualization, a process essential for eventual blastocyst implantation. The importance of immunophilins to steroid receptor action was therefore reinforced by the observation that immunophilins appear to be hormonally regulated in cycling pre-menopausal human endometrium. Further studies into the effects of immunophilin loss and knockdown on steroid receptor-mediated responses in specific mouse tissues, knockout-derived mouse embryo fibroblasts and cancer cell lines may contribute to our understanding of the receptor-selective and tissue-specific actions of the immunophilins. Elucidation of the mechanisms through which they modulate receptor function may provide opportunities for therapeutic intervention in steroid-related disease.
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Warrier, Manya. "Role of FKBP51 and FKBP52 in Glucocorticoid Receptor Regulated Metabolism." University of Toledo Health Science Campus / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=mco1223923687.

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Sandhu, Khushwant Singh. "Identification and molecular characterization of the putative immunophilins (IMMs) in the oilseed rape pathogens Leptosphaeria maculans, Leptosphaeria biglobosa, and Plasmodiophora brassicae." Doctoral thesis, Česká zemědělská univerzita v Praze, 2016. http://www.nusl.cz/ntk/nusl-259691.

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Oilseed rape is largely infected by several phytopathogens and two most economical important diseases are blackleg caused by fungus species complex Leptosphaeria maculans and L. biglobosa and clubroot caused by protist P. brassicae. The sequenced genomes of these phytopathogens provide opportunity to uncover various aspects related to disease infection, host pathogen interactions, plant disease resistance, and evolution of pathogens. Considering these we focused on one of the most conserved family called immunophilins (IMMs) in these genomes. IMMs are comprised of three structurally unrelated sub-families including cyclophilins (CYPs), FK506-binding proteins (FKBPs), and parvulin-like proteins (PARs). We identified putative members of IMMs in each phytopathogen using bioinformatics approaches. We further characterized the IMMs based on domain architecture, subcellular localization, exon-intron organization, transcriptomic expression patterns, gene ontology terms, conserved motifs presents and evolutionary analyses. IMMs are performing several vital roles in plants, animals and fungi. However, in phytopathogens their roles are not well established except for cyclophilin that implicates in pathogenicity in some phytopathogens. Therefore, we exploited the role of cyclophilin in L. maculans and L. biglobosa using expression profiles and in P. brassicae using Magnaporthe oryzae cyclophilin deletion mutant. Overall, we concluded that the cyclophilin acts as a virulence determinant in our studied phytopathogens. However, delineating the precise role of other IMMs would also be imperative. Taken together, our findings for the first time shed light on the highly conserved IMM family in the oilseed rape pathogens.
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Somarelli, Jason Andrew. "The Role of Splicing Factors and Small Nuclear RNAS in Spliceosomal Formation." FIU Digital Commons, 2009. http://digitalcommons.fiu.edu/etd/83.

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Protein coding genes are comprised of protein-coding exons and non-protein-coding introns. The process of splicing involves removal of the introns and joining of the exons to form a mature messenger RNA, which subsequently undergoes translation into polypeptide. The spliceosome is a large, RNA/protein assembly of five small nuclear RNAs as well as over 300 proteins, which catalyzes intron removal and exon ligation. The selection of specific exons for inclusion in the mature messenger RNA is spatio-temporally regulated and results in production of an enormous diversity of polypeptides from a single gene locus. This phenomenon, known as alternative splicing, is regulated, in part, by protein splicing factors, which target the spliceosome to exon/intron boundaries. The first part of my dissertation (Chapters II and III) focuses on the discovery and characterization of the 45 kilodalton FK506 binding protein (FKBP45), which I discovered in the silk moth, Bombyx mori, as a U1 small nuclear RNA binding protein. This protein family binds the immunosuppressants FK506 and rapamycin and contains peptidyl-prolyl cis-trans isomerase activity, which converts polypeptides from cis to trans about a proline residue. This is the first time that an FKBP has been identified in the spliceosome. The second section of my dissertation (Chapters IV, V, VI and VII) is an investigation of the potential role of small nuclear RNA sequence variants in the control of splicing. I identified 46 copies of small nuclear RNAs in the 6X whole genome shotgun of the Bombyx mori p50T strain. These variants may play a role in differential binding of specific proteins that mediate alternative splicing. Along these lines, further investigation of U2 snRNA sequence variants in Bombyx mori demonstrated that some U2 snRNAs preferentially assemble into high molecular weight spliceosomal complexes over others. Expression of snRNA variants may represent another mechanism by which the cell is able to fine tune the splicing process.
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Books on the topic "Immunophilins"

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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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Moore, Stephen. Characterisation of a novel immunophilin-like gene, repressed by low doses of ionising radiation: Identification of interacting proteins. [S.l: The author], 2002.

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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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Bultynck, Geert. Intracellular Ca2+-Release Channels As Cellular Targets for Immunophilins: A Molecular, Functional, and Structural Analysis (Acta Biomedica Lovaniensia, 249). Leuven Univ Pr, 2001.

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Immunosuppressant Analogs in Neuroprotection. Humana Press, 2002.

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V, Borlongan Cesario, Isacson Ole, and Sanberg Paul R, eds. Immunosuppressant analogs in neuroprotection. Totowa, N.J: Humana Press, 2003.

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V, Borlongan Cesario, Isacson Ole, and Sanberg Paul R, eds. Immunosuppressant analogs in neuroprotection. Totowa, N.J: Humana Press, 2003.

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V, Borlongan Cesario, Isacson Ole, and Sanberg Paul R, eds. Immunosuppressant analogs in neuroprotection. Totowa, N.J: Humana Press, 2003.

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Book chapters on the topic "Immunophilins"

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Galat, Andrzej. "Peptidylproline cis-trans-isomerases: immunophilins." In EJB Reviews 1993, 153–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78757-7_13.

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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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Bianchin, Alessandra, Anthony J. Chubb, and Angus Bell. "Immunophilins as Possible Drug Targets in Apicomplexan Parasites." In Comprehensive Analysis of Parasite Biology: From Metabolism to Drug Discovery, 193–212. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2016. http://dx.doi.org/10.1002/9783527694082.ch8.

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Klee, Claude B. "Structure of Calcineurin and Its Complex with Immunophilins." In Calcium Homeostasis, 125–41. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-58306-3_6.

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Rahamimoff, Hannah, Benayahu Elbaz, Michael Valitsky, Mahdi Khatib, Marina Eskin-Schwartz, and Daniela Elmaz. "Immunosuppressive Drugs, Immunophilins, and Functional Expression of NCX Isoforms." In Advances in Experimental Medicine and Biology, 275–87. Boston, MA: Springer US, 2012. http://dx.doi.org/10.1007/978-1-4614-4756-6_23.

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Barik, Sailen. "Novel Apicomplexan Phosphatases and Immunophilins as Domain-Specific Drug Targets." In Apicomplexan Parasites, 287–306. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527633883.ch15.

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Shi, Lujing, and Aigen Fu. "Plant Immunophilins: A Protein Family with Diverse Functions Beyond Protein Folding Activity." In Elucidation of Abiotic Stress Signaling in Plants, 367–95. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2211-6_14.

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Cox, Marc B., and Jill L. Johnson. "The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function." In Methods in Molecular Biology, 45–66. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-295-3_4.

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Bierer, Barbara E. "Cyclosporin A, FK506, and Rapamycin: Binding to Immunophilins and Biological Action (Part 1 of 2)." In Chemical Immunology and Allergy, 128–41. Basel: KARGER, 1994. http://dx.doi.org/10.1159/000319251.

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Conference papers on the topic "Immunophilins"

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Kadeba, Pierre, Hairu Chen, Songwei Wu, Jonathan G. Scammell, and Donna L. Cioffi. "Regulation Of Pulmonary Endothelial Store-Operated Calcium Entry By Fk506-Binding Immunophilins." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1946.

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Cioffi, DL. "Differential Expression of Immunophilin FKBP51 in Pulmonary Endothelium." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2345.

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Peteranderl, C., L. Sauerhering, L. Meier, B. Nganko, A. Kupke, B. Selvakumar, S. Becker, and S. Herold. "Targeting Immunophilin- and MAPK-Associated Pathways to Inhibit MERS-CoV Replication and Prevent Lung Injury." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5759.

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Lowe, Eric, and Shirin Arastu-Kapur. "Abstract 1738: Decreases in ubiquitin levels post proteasome inhibition identify FKBP4 immunophilin as a novel target for potentiating the anti-myeloma activity of carfilzomib." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1738.

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Reports on the topic "Immunophilins"

1

Luan, Sheng. Immunophilins and their function in photosystem II assembly. Office of Scientific and Technical Information (OSTI), November 2012. http://dx.doi.org/10.2172/1055782.

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