Littérature scientifique sur le sujet « FKBP12 protein »
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Articles de revues sur le sujet "FKBP12 protein"
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 et Wei-Jan Wang. « Penetrating Exploration of Prognostic Correlations of the FKBP Gene Family with Lung Adenocarcinoma ». Journal of Personalized Medicine 13, no 1 (26 décembre 2022) : 49. http://dx.doi.org/10.3390/jpm13010049.
Texte intégralZENG, Baifei, J. Randy MACDONALD, G. James BANN, Konrad BECK, E. Jay GAMBEE, A. Bruce BOSWELL et 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 (15 février 1998) : 109–14. http://dx.doi.org/10.1042/bj3300109.
Texte intégralBarg, S., J. A. Copello et 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 (1 mai 1997) : C1726—C1733. http://dx.doi.org/10.1152/ajpcell.1997.272.5.c1726.
Texte intégralChen, Hui, Sourajit M. Mustafi, David M. LeMaster, Zhong Li, Annie Héroux, Hongmin Li et Griselda Hernández. « Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6 ». Acta Crystallographica Section D Biological Crystallography 70, no 3 (15 février 2014) : 636–46. http://dx.doi.org/10.1107/s1399004713032112.
Texte intégralBultynck, Geert, Daniela Rossi, Geert Callewaert, Ludwig Missiaen, Vincenzo Sorrentino, Jan B. Parys et 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 (11 octobre 2001) : 47715–24. http://dx.doi.org/10.1074/jbc.m106573200.
Texte intégralVervliet, Tim, Jan B. Parys et 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 (1 juin 2015) : 396–404. http://dx.doi.org/10.1042/bst20140298.
Texte intégralOzawa, Terutaka. « Effects of FK506 on Ca2+ Release Channels (Review) ». Perspectives in Medicinal Chemistry 2 (janvier 2008) : PMC.S382. http://dx.doi.org/10.4137/pmc.s382.
Texte intégralDolinski, Kara J., et Joseph Heitman. « Hmo1p, a High Mobility Group 1/2 Homolog, Genetically and Physically Interacts With the Yeast FKBP12 Prolyl Isomerase ». Genetics 151, no 3 (1 mars 1999) : 935–44. http://dx.doi.org/10.1093/genetics/151.3.935.
Texte intégralTang, Wang-Xian, Ya-Fei Chen, Ai-Ping Zou, William B. Campbell et 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 (1 avril 2002) : H1304—H1310. http://dx.doi.org/10.1152/ajpheart.00843.2001.
Texte intégralReiken, 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 (10 mars 2003) : 919–28. http://dx.doi.org/10.1083/jcb.200211012.
Texte intégralThèses sur le sujet "FKBP12 protein"
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.
Texte intégralZibrova, 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.
Texte intégralMain, 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.
Texte intégralChaurasia, 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.
Texte intégralKim, 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.
Texte intégralTitle 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
De, Cicco Maristella Verfasser], Sonja A. [Akademischer Betreuer] [Gutachter] Dames et 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.
Texte intégralDavies, 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.
Texte intégralOlivieri, 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.
Texte intégralFKBP12 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
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.
Texte intégralWe 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
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.
Texte intégralChapitres de livres sur le sujet "FKBP12 protein"
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) ». Dans Encyclopedia of Signaling Molecules, 1596. New York, NY : Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101146.
Texte intégralD’Arrigo, Paolo, Martina Tufano, Anna Rea, Simona Romano et Maria Fiammetta Romano. « FKBP (FK506 Binding Protein) ». Dans Encyclopedia of Signaling Molecules, 1737–67. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101769.
Texte intégralD’Arrigo, Paolo, Martina Tufano, Anna Rea, Simona Romano et Maria Fiammetta Romano. « FKBP (FK506 Binding Protein) ». Dans 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.
Texte intégralKatoh, Masaru, Giorgio Berton, Anna Baruzzi, Jennifer Boylston, Charles Brenner, Yong-Hun Lee, William Schiemann et al. « FKBP-Rapamycin-Associated Protein (FRAP) ». Dans Encyclopedia of Signaling Molecules, 623. New York, NY : Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100450.
Texte intégralCowling, Rachel J., Paola Vittorioso, Jean-Denis Faure, Michel Caboche et Catherine Bellini. « The role of PASTICCINO1, an FKBP-like protein, in plant development ». Dans 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.
Texte intégral« Rapamycin and FKBP12 Target-1 Protein (RAFT1) ». Dans Encyclopedia of Signaling Molecules, 4462. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103220.
Texte intégralKrakow, Deborah, et Yasemin Alanay. « FKBP10 (FKBP65 Protein), Osteogenesis Imperfecta and Bruck Syndrome ». Dans Osteogenesis Imperfecta, 151–57. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-397165-4.00015-0.
Texte intégral« FKBP-Rapamycin-Associated Protein (FRAP) ». Dans Encyclopedia of Signaling Molecules, 1767. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101274.
Texte intégralBuchner, Johannes, Tina Weikl, Hans Bügl, Franziska Pirkl et Suchira Bose. « [33] Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52 ». Dans Methods in Enzymology, 418–29. Elsevier, 1998. http://dx.doi.org/10.1016/s0076-6879(98)90035-0.
Texte intégralActes de conférences sur le sujet "FKBP12 protein"
Ioris, R. Maciel. « PO-108 FKBP10 is an oncofetal protein that supports lung cancer growth by promoting protein translation elongation ». Dans 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.
Texte intégralKomaragiri, Shravan Kumar. « Abstract 3061 : Role of ID4 (inhibitor of DNA binding protein 4) in FKBP52-AR pathway ». Dans 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.
Texte intégralKomaragiri, Shravan Kumar. « Abstract 3061 : Role of ID4 (inhibitor of DNA binding protein 4) in FKBP52-AR pathway ». Dans 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.
Texte intégralRatz, Veronika, Anne-Christine Plank, Anja Schulze-Krebs et Stephan von Hörsten. « A13 Expression of FKBP51 and HAP40 protein in a congenic rat model of huntington disease ». Dans EHDN 2018 Plenary Meeting, Vienna, Austria, Programme and Abstracts. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/jnnp-2018-ehdn.13.
Texte intégralRomano, Simona, Antonio Sorrentino, AnnaLaura Di Pace, Stefania Staibano, Massimo Mascolo, Rita Bisogni, Gennaro Ilardi et Maria Fiammetta Romano. « Abstract 4999 : FK506 binding protein 51 (FKBP51) sustains stemness and the metastatic potential of malignant melanoma ». Dans 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.
Texte intégralAlqudah, A., R. McNally, N. Todd, DJ Grieve, T. Robson et L. McClements. « 4 The role of a novel anti-angiogenic protein, FKBPL, in angiogenesis associated with cardiac dysfunction ». Dans 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.
Texte intégralStorer, CL, K. Olivares, RJ Fletterick, P. Webb et 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 ». Dans 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.
Texte intégralMroz, Robert M., Adam Holownia, Elzbieta Chyczewska et Jan J. Braszko. « Heat Shock Proteins And FKBP51 Expression In Sputum Cells Of COPD Patients During Formoterol/Corticosteroid/Theophylline Therapy ». Dans 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.
Texte intégralRomano, Simona, Giovanna Nappo, Elena Cesaro, Antonio Candela et 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. » Dans 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.
Texte intégralRomano, Simona, Anna Laura Di Pace, Antonio Sorrentino, Giovanna Nappo, Rosanna Martinelli, Rita Bisogni et Maria Fiammetta Romano. « Abstract 260 : FK506 binding protein (FKBP) 51 controls “TNF-related apoptosis inducing ligand” (TRAIL) response in melanoma ». Dans 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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