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90 documents found
1: Title: Membrane proteome characterization of periodontal ligament cell sets from deciduous and permanent teeth.
Authors: Giovani, Priscila A, et.al. .
Journal: Journal of periodontology (J Periodontol), 2018 .
Snippet: RESULTS: Comparative gene ontology enrichment analysis evidenced that most stickling differences involved "endomembrane system" (PICALM, STX4, and LRP10), "hydrolase activity" (NCSTN and XRCC6), "protein binding" (PICALM, STX4, GPNMB, VASP, extended-synaptotagmin 2 [ESYT2], and leucine-rich repeat containing 15 [LRRC15]), and "isomerase activity" (FKBP8).
Affiliation: Department of Pediatric Dentistry, Piracicaba Dental School, University of Campinas, Campinas, São Paulo, Brazil. Department of Prosthodontics and Periodontics, Division of Periodontics, Piracicaba Dental School, University of Campinas, Piracicaba, São Paulo, Brazil. Brazilian Biosciences National Laboratory, LNBio, CNPEM, Campinas, São Paulo, Brazil. Department of Genetics, Evolution and Bioagents, Institute of Biology, University of Campinas, Piracicaba, São Paulo, Brazil. Department of Dental Materials, São Leopoldo Mandic Research Center, Campinas, São Paulo, Brazil. .
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2: Title: FKBP8 Enhances Protein Stability of the CLC-1 Chloride Channel at the Plasma Membrane.
Authors: Peng, Yi-Jheng, et.al. .
Journal: International journal of molecular sciences (Int J Mol Sci), Vol. 19 (12), 2018 .
Snippet: Immunoblotting analyses of plasma membrane proteins purified from skeletal muscle further confirm surface localization of FKBP8.
Affiliation: Department of Physiology, College of Medicine, National Taiwan University, Taipei 10051, Taiwan. yijhengp@usc.edu. Department of Physiology, College of Medicine, National Taiwan University, Taipei 10051, Taiwan. angela2747@yahoo.com.tw. Department of Physiology, College of Medicine, National Taiwan University, Taipei 10051, Taiwan. d01441001@ntu.edu.tw. Department of Physiology, College of Medicine, National Taiwan University, Taipei 10051, Taiwan. wingtalk1006@hotmail.com. Institute of Anatomy and Cell Biology, School of Medicine, National Yang-Ming University, Taipei 10051, Taiwan. cassis0211@hotmail.com. Neuroscience Center, University of California, Davis, CA 95616, USA. tycchen@ucdavis.edu. Institute of Anatomy and Cell Biology, School of Medicine, National Yang-Ming University, Taipei 10051, Taiwan. cjjeng@ym.edu.tw. Brain Research Center, National Yang-Ming University, Taipei 12212, Taiwan. cjjeng@ym.edu.tw. Department of Physiology, College of Medicine, National Taiwan University, Taipei 10051, Taiwan. tang@ntu.edu.tw. Graduate Institute of Brain and Mind Sciences, College of Medicine, National Taiwan University, Taipei 10051, Taiwan. tang@ntu.edu.tw. .
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3: Title: Signal peptide peptidase promotes tumor progression via facilitating FKBP8 degradation.
Authors: Hsu, Fu-Fei, et.al. .
Journal: Oncogene, 2018 .
Snippet: Quantitative analysis of the proteomic changes of microsomal proteins in lung cancer cells by the stable isotope labeling with amino acids in cell culture (SILAC) approach revealed that the level of FKBP8, an endogenous inhibitor of mTOR, was significantly increased following SPP depletion.
Affiliation: Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan. Cancer Center, Shuang Ho Hospital, Taipei Medical University, Taipei, Taiwan. Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan. lyc@ibms.sinica.edu.tw. .
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4: Title: FKBP8 inhibits virus-induced RLR-VISA signaling.
Authors: Xu, Shan-Shan, et.al. .
Journal: Journal of medical virology (J Med Virol), Vol. 91 (3): 482-492, 2019 .
Snippet: Notably, FKBP8 also promoted the degradation of TBK1, RIG-I, and TRAF3 resulting from FKBP8 reinforced Sendai virus-induced endogenous polyubiquitination of RIG-I, TBK1, and TNF receptor-associated factor 3 (TRAF3).
Affiliation: Key Laboratory of Functional Small Organic Molecules, Ministry of Education and College of Life Science, Jiangxi Normal University, Nanchang, China. Jiangxi Key Laboratory of Nanomaterials and Sensors, School of Physics, Communication and Electronics, Jiangxi Normal University, Nanchang, China. .
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5: Title: ZMYND10 functions in a chaperone relay during axonemal dynein assembly.
Authors: Mali, Girish R, et.al. .
Journal: eLife, Vol. 7, 2018 .
Snippet: Through the use of mouse genetics, imaging and quantitative proteomics we uncover that ZMYND10 is a novel co-chaperone that confers specificity for the FKBP8-HSP90 chaperone complex towards axonemal dynein clients required for cilia motility.
Affiliation: MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom. Laboratory Animal Resource Centre, University of Tsukuba, Tsukuba, Japan. Centre for Integrative Physiology, University of Edinburgh, Edinburgh, United Kingdom. Division of Molecular and Clinical Medicine, University of Dundee, Dundee, United Kingdom. System Biology Ireland, University College Dublin, Dublin, Ireland. Department of Biological Sciences, University of Tokyo, Tokyo, Japan. Institute for Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany. Systems Biology Ireland, University College Dublin, Dublin, Ireland. .
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6: Title: Comparative genomic analysis of intracranial germ cell tumors - the preliminary study focused on Sonic Hedgehog signaling pathway.
Authors: Kuleszo, Dominika, et.al. .
Journal: Contemporary oncology (Poznan, Poland) (Contemp Oncol (pozn)), Vol. 21 (4): 279-284, 2017 .
Snippet: Moreover, both tumors showed various copy gain of genes being ligands, regulators, receptors or target genes of SHh (MTSS1; PRKACA and FKBP8) as well as gain of genes of SHh coopting WNT pathway (WNT3, WNT5B, WNT9B in both tumors; WNT16, WNT2 in pineal lesion).
Affiliation: Department of Biology and Medical Genetics, Cinical Genetics Unit, Medical University of Gdańsk, Gdansk, Poland. Department of Pathology, Children's Health Memorial Institute, Warsaw, Poland. Department of Pediatrics, Oncology and Hematology, Medical University of Gdańsk, Gdansk, Poland. Department of Oncology, Children's Health Memorial Institute, Warsaw, Poland. Department of Neurosurgery, Children's Health Memorial Institute, Warsaw, Poland. Department of Pathology and Neuropathology, Medical University of Gdańsk, Gdansk, Poland. .
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7: Title: NMR analysis of the backbone dynamics of the small GTPase Rheb and its interaction with the regulatory protein FKBP38.
Authors: De Cicco, Maristella, et.al. .
Journal: FEBS letters (Febs Lett), Vol. 592 (1): 130-146, 2018 .
Snippet: Ras homolog enriched in brain (Rheb) is a small GTPase that regulates mammalian/mechanistic target of rapamycin complex 1 (mTORC1) and, thereby, cell growth and metabolism.
Affiliation: Technische Universität München, Department of Chemistry, Biomolecular NMR Spectroscopy, Garching, Germany. Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany. .
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8: Title: FKBP8 protects the heart from hemodynamic stress by preventing the accumulation of misfolded proteins and endoplasmic reticulum-associated apoptosis in mice.
Authors: Misaka, Tomofumi, et.al. .
Journal: Journal of molecular and cellular cardiology (J Mol Cell Cardiol), Vol. 114, 2018 .
Snippet: Immunocytological and immunoprecipitation analyses indicate that FKBP8 is localized to the ER and mitochondria in the isolated cardiomyocytes, interacting with heat shock protein 90.
Affiliation: The School of Cardiovascular Medicine and Sciences, King's College London British Heart Foundation Centre of Research Excellence, London SE5 9NU, UK. Developmental Biology, Laboratory Animal Science, The Institute of Experimental Animal Sciences, Osaka University Medical School, Suita 565-0871, Japan. Department of Cardiovascular Medicine, Osaka University Graduate School of Medicine, Suita 565-0871, Japan. Department of Genome Biology, Osaka University Graduate School of Medicine, Suita 565-0871, Japan. The School of Cardiovascular Medicine and Sciences, King's College London British Heart Foundation Centre of Research Excellence, London SE5 9NU, UK. Electronic address: kinya.otsu@kcl.ac.uk. .
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9: Title: Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.
Authors: De Cicco, Maristella, et.al. .
Journal: Protein science : a publication of the Protein Society (Protein Sci), Vol. 27 (2): 546-560, 2018 .
Snippet: Thus, they may be used as membrane anchors if the full y1fatc sequence is disturbing or if a chemically synthesized y1fatc peptide shall be attached by native chemical ligation, for example, unlabeled peptide to 15 N-labeled target protein for NMR studies.
Affiliation: Department of Chemistry, Technische Universität München, Biomolecular NMR Spectroscopy, Garching, Germany. Department of Biomedical Technology, Laboratory of Chemical Biology, Technische Universiteit Eindhoven, Eindhoven, The Netherlands. Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany. .
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10: Title: Parkin-independent mitophagy-FKBP8 takes the stage.
Authors: Lim, Grace Gy, et.al. .
Journal: EMBO reports (Embo Rep), Vol. 18 (6): 864-865, 2017 .
Snippet: The authors demonstrate that FKBP8 interacts preferentially with LC3A via its LIR motif to destroy damaged mitochondria.
Affiliation: Neurodegeneration Research Laboratory, National Neuroscience Institute, Singapore City, Singapore. Department of Physiology, National University of Singapore, Singapore City, Singapore. Duke-NUS Medical School, Singapore City, Singapore. .
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11: Title: FKBP8 recruits LC3A to mediate Parkin-independent mitophagy.
Authors: Bhujabal, Zambarlal, et.al. .
Journal: EMBO reports (Embo Rep), Vol. 18 (6): 947-961, 2017 .
Snippet: FKBP8 (also known as FKBP38), a unique member of the FK506-binding protein (FKBP) family, is similarly anchored in the OMM and acts as a multifunctional adaptor with anti-apoptotic activity.
Affiliation: Molecular Cancer Research Group, Department of Medical Biology, University of Tromsø -The Arctic University of Norway, Tromsø, Norway. Merck KGaA, Darmstadt, Germany. Molecular Cancer Research Group, Department of Medical Biology, University of Tromsø -The Arctic University of Norway, Tromsø, Norway terje.johansen@uit.no. .
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12: Title: The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90.
Authors: Blundell, Katie L I M, et.al. .
Journal: PloS one, Vol. 12 (3): e0173543, 2017 .
Snippet: FKBP8 binding to Hsp90 did not substantially influence its ATPase activity.
Affiliation: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RQ, England. .
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13: Title: Identification of proteins suppressing the functions of oncogenic phosphatase of regenerating liver 1 and 3.
Authors: Lee, Ju-Dong, et.al. .
Journal: Experimental and therapeutic medicine (Exp Ther Med), Vol. 12 (5): 2974-2982, 2016 .
Snippet: Alignment with the NCBI BLAST database revealed 12 interactive proteins: Synaptic nuclear envelope protein 2, emerin, mannose 6-phosphate receptor-binding protein 1, low-density lipoprotein receptor-related protein 10, Rab acceptor 1, tumor protein D52-like 2, selectin P ligand (SELPLG), guanylate binding protein 1, transmembrane and ubiquitin-like domain-containing 2, NADH:ubiquinone oxidoreductase subunit B8, syndecan 4 and FK506-binding protein 8 (FKBP8).
Affiliation: Graduate School of Medical Science and Engineering, Biomedical Research Center, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Republic of Korea. Immunotherapy Convergence Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Republic of Korea. New Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu 701-310, Republic of Korea. .
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14: Title: Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90β.
Authors: Peng, Yi-Jheng, et.al. .
Journal: Scientific reports (Sci Rep), Vol. 6, 2016 .
Snippet: We identified three CLC-1-interacting proteins that are well-known heat shock protein 90 (Hsp90)-associated co-chaperones: FK506-binding protein 8 (FKBP8), activator of Hsp90 ATPase homolog 1 (Aha1), and Hsp70/Hsp90 organizing protein (HOP).
Affiliation: Department of Physiology, College of Medicine, National Taiwan University, Taipei, Taiwan. Department of Medical Research, National Taiwan University Hospital, Taipei, Taiwan. Neuroscience Center, University of California, Davis, USA. Graduate Institute of Brain and Mind Sciences, College of Medicine, National Taiwan University, Taipei, Taiwan. .
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15: Title: Expanding the Interactome of the Noncanonical NF-κB Signaling Pathway.
Authors: Willmann, Katharina L, et.al. .
Journal: Journal of proteome research (J Proteome Res), Vol. 15 (9): 2900-9, 2016 .
Snippet: We provide validation of the novel NIK and IKKα interactor FKBP8, which may regulate processes downstream of noncanonical NF-κB signaling.
Affiliation: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences , 1090 Vienna, Austria. Department of Medicine I, Laboratory of Infection Biology, Medical University of Vienna , 1090 Vienna, Austria. Department of Paediatrics and Adolescent Medicine, Medical University of Vienna , 1090 Vienna, Austria. Ludwig Boltzmann Institute for Rare and Undiagnosed Diseases and CeRUD Vienna Center for Rare and Undiagnosed Diseases , 1090 Vienna, Austria. .
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16: Title: A telomerase-derived peptide regulates reactive oxygen species and hepatitis C virus RNA replication in HCV-infected cells via heat shock protein 90.
Authors: Lee, Seoung-Ae, et.al. .
Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun), Vol. 471 (1): 156-62, 2016 .
Snippet: Importantly, GV1001 suppressed HCV RNA replication in JFH-1 cells by inhibiting the binding of HSP90 to FKBP8, a member of the FK506-binding protein family.
Affiliation: Department of Microbiology and Immunology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea. Department of Anatomy and Cell Biology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Department of Biomedical Laboratory Science, College of Health Science, Cheongju University, Cheongju 28503, Republic of Korea. Department of Anatomy and Cell Biology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea. Digestive Disease Center and Research Institute, SoonChunHyang University Bucheon Hospital, Bucheon 14584, Republic of Korea. Department of Microbiology and Immunology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Cancer Research Institute, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Medical Research Institute for Infectious Diseases, Seoul National University College of Medicine, Seoul 03080, Republic of Korea. Department of Microbiology and Immunology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Cancer Research Institute, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Medical Research Institute for Infectious Diseases, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Republic of Korea. Medical Research Institute for Infectious Diseases, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Department of Anatomy and Cell Biology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Republic of Korea. Electronic address: hangrae2@snu.ac.kr. Department of Microbiology and Immunology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Cancer Research Institute, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Liver Research Institute, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Medical Research Institute for Infectious Diseases, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Republic of Korea. Electronic address: kbumjoon@snu.ac.kr. .
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17: Title: FKBP8 interact with classical swine fever virus NS5A protein and promote virus RNA replication.
Authors: Li, Helin, et.al. .
Journal: Virus genes, Vol. 52 (1): 99-106, 2016 .
Snippet: These data suggest that FKBP8 plays a critical role in the viral life cycle, particularly during the virus RNA replication period.
Affiliation: College of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, People's Republic of China. College of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, People's Republic of China. zcc87051007@126.com. .
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18: Title: Involvement of FKBP6 in hepatitis C virus replication.
Authors: Kasai, Hirotake, et.al. .
Journal: Scientific reports (Sci Rep), Vol. 5, 2015 .
Snippet: HCV infection promoted the expression of FKBP6, but not that of FKBP8, in cultured cells and human liver tissue.
Affiliation: Department of Microbiology, Faculty of Medicine, University of Yamanashi, Chuo-shi, Yamanashi 409-3898, Japan. Faculty of Life and Environmental Sciences, University of Yamanashi, Kofu-shi, Yamanashi 400-8510, Japan. Institute of Medical Chemistry, Hoshi University, 2-4-41 Ebara, Shinagawa-ku, Tokyo 142-8501, Japan. Department of Anatomy and Cell Biology, Division of Medicine, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Chuo-shi, Yamanashi 409-3898, Japan. Department of First Surgery, Faculty of Medicine, University of Yamanashi, Chuo-shi, Yamanashi 409-3898, Japan. First Department of Internal Medicine, Faculty of Medicine, University of Yamanashi, Chuo-shi, Yamanashi 409-3898, Japan. Department of Tumor Virology, Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama University, Okayama, Okayama 700-8530, Japan. Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan. Department of Gastroenterology and Hepatology, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido 060-8638, Japan. .
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19: Title: Silencing FKBP38 gene by siRNA induces activation of mTOR signaling in goat fetal fibroblasts.
Authors: Fu, Y T, et.al. .
Journal: Genetics and molecular research : GMR (Genet Mol Res), Vol. 14 (3): 9675-82, 2015 .
Snippet: FKBP38 (also known as FKBP8) is a unique member of the FK506-binding protein (FKBP) family, and its role is controversial because it acts as an upstream regulator of the mTOR signaling pathway, which controls cell growth, proliferation, and differentiation.
Affiliation: College of Life Sciences, Inner Mongolia University, Hohhot, China. College of Life Sciences, Inner Mongolia University, Hohhot, China lswzg@imu.edu.cn. .
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20: Title: Role of mTOR1 and mTOR2 complexes in MEG-01 cell physiology.
Authors: López, Esther, et.al. .
Journal: Thrombosis and haemostasis (Thromb Haemostasis), Vol. 114 (5): 969-81, 2015 .
Snippet: Since mTOR associates with different proteins to form two functional macromolecular complexes, we aimed to investigate the role of the mTOR1 and mTOR2 complexes in MEG-01 cell physiology in response to thrombopoietin (TPO).
Affiliation: Pedro Cosme Redondo Liberal, PhD, Department of Physiology, University of Extremadura, Avd. de la Universidad s/n PD. 10003 , Cáceres, Spain, Tel.: +34 927 25 71 06 ext.: 5 15 22, Fax: +34 927 25 71 10, E-mail: pcr@unex.es. .
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