Relevant bibliographies by topics / Immunophilins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
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Academic literature on the topic 'Immunophilins'

Author: Grafiati
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 subfa
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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 clearl
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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
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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
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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
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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 <i>Caenorhabditis elegans </i>(<i>C. elegans</i>) has recently been reported. Cyclophilin 3 (
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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
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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.<br>"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
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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
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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 si
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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"

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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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