|
[1] Sat S T T, Kochel S K K, Irie S, et al.Cloning and functional analysis ofBAG-l: A novel Bcl-2-binding protein with anti-cell death activity. Cell, 1995, 80(2): 279-284.
[2] Brive L, Takayama S, Homma S, et al. The carboxyl-terminal lobe of Hsc70 ATPase domain is sufficient for binding to BAG1. Biochem Biophys Res Commun, 2001, 289(5): 1099-1105.
[3] Doong H, Vrailas A, Kohn E C. What's in the ‘BAG'? - a functional domain analysis of the BAG- family proteins. Cancer Letters, 2002, 18(2): 25-32.
[4] Reed J C, Kathryn R, Knee D A, et al. Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Nature Structure Biology, 2001, 8(4): 349-352.
[5] Zhen X, Page R C, Gomes M M, et al. Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2. Nature Structure & Molecular Biology, 2008, 15(2): 1308-1317.
[6] Ozawa F, Friess H, Zimmermann A, et al. BAG4:SODD protein contains a short BAG domain. The Journal of Biological Chemistry, 2002, 277 (23): 409-413.
[7] Brockmann C, Leitner D, Labudde D, et al. The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains. FEBS Letters, 2004, 558(1-3): 101-106.
[8] Arakawa A, Handa N, Ohsawa N, et al. The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure, 2010, 18(3): 309-319.
[9] Janina B, Joachim K. BAG-6, a jack of all trades in health and disease. Cell Mol Life Sci, 2014, 71(10): 1829-1837.
[10] Mink S, Andrew C B, Cato, et al. BAG-1 family of cochaperones in the modulation of nuclear receptor action. Journal of Steroid Biochemistry & Molecular Biology, 2001, 78(2): 379-388.
[11] Verghese S, Harris J R, Balla T, et al. The Networking of chaperones by co-chaperones control of cellular protein homeostasis. Subcellular Biochemistry, 2014, 78(2): 1731-1737.
[12] Rosati A, Basile A, Falco A, et al. Role of BAG3 protein in leukemia cell survival and response to therapy. Biochim Biophys Acta, 2012, 26(2): 365-369.
[13] Antoku K, Maser R S, Delach S M, et al. Isolation of Bcl-2 binding proteins that exhibit homology with BAG-1 and suppressor of death domains protein. Biochem Biophys Res Commun, 2001, 286(5):1003-1010.
[14] Bimston D, Song Jaewhan, Winchester D, et al. BAG-1 a negative regulator of Hsp70. The EMBO Journal, 1998, 17 (23): 6871-6878.
[15] Ni W K, Chen B Y, Zhou G X, et al. Overexpressed nuclear BAG-1 in human hepatocellular carcinoma is associated with poor prognosis and resistance to doxorubicin. J Cell Biochem, 2013, 114(9): 2120-2130.
[16] Shinichi Takayama, John C R. Molecular chaperone targeting and regulationby BAG family proteins. Nature Cell Biology, 2001, 3(2): 237-241.
[17] Arndt V, Daniel C, Nastainczyk W, et al. BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Molecular Biology of the Cell, 2005, 16(2): 5891-5900.
[18] Homma S, Lwasaki M, Takayama S, et al. BAG3 deficiency results in fulminant myopathy and early lethality. Am J Pathol, 2006, 169(3): 761-773.
[19] Kwon K R, Ahn J Y, Kim J Y, et al. Disruption of bis leads to the deterioration of the vascular niche for hematopoietic stem cells. Stem Cells, 2010, 28(2): 268-278.
[20] Jiang Y P, Woronicz J D, Liu W, et al. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science, 1999, 283(22): 543-546.
[21] Kalia L V, Kalia S K, Chau H, et al. Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5). PLoS One, 2011, 6(2): e14695.
[22] Krenciute G, Liu S F, Liu Q M, et al. Nuclear BAG6-UBL4A-GET4 complex mediates DNA damage signaling and cell death. J Biol Chem, 2013, 288(28): 20547-20557.
[23] Wang Y D, Cheng J, Zhang W L, et al. The role of expression and polymorphism of the BAG-1 gene in response to platinum-based chemotherapeutics in NSCLC. Oncol Rep, 2012, 27(4): 979-986.
[24] Wang H Q, Zhang H Y, Meng X, et al. Induction of BAG2 protein during proteasome inhibitor-induced apoptosis in thyroid carcinoma cells. Br J Pharmacol, 2008, 155(5): 655-660.
[25] Sun N F, Meng Q Y, Tian A. Expressions of the anti-apoptotic genes Bag-1 and Bcl-2 in colon cancer and their relationship. Am J Surg, 2010, 200(3): 341-345.
[26] Liu H Y, Wang Z M, Bai Y, et al. Different BAG-1 isoforms have distinct functions in modulating chemotherapeutic-induced apoptosis in breast cancer cells. Acta Pharmacologica Sinica, 2009, 30(2): 235-241.
[27] Kudoh M, Knee D A, Takayama S, et al. Bag1 proteins regulate growth and survival of ZR-75-1 human breast cancer cells. Cancer Research, 2002, 62(2): 1904-1909.
[28] Ozawa F, Friess H, Kleeff J, et al. Enhanced expression of silencer of death domains (SODD/BAG-4) in pancreatic cancer. Biochem Biophys Res Commun, 2000, 271(2): 409-413.
[29] Karlheinz M, Eric Edsinger.The Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis. Mann ans Edsinger Proteome Science, 2014, 12(28): 1001-1012.
[30] Pawel L, Stephen H. SGTA antagonizes BAG6-mediated protein triage. PNAS, 2012, 109(47): 19214-19219.
[31] Winnefeld M, Grewening A, Cziepluch C, et al. Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest. Exp Cell Res, 2006, 312(13): 2500-2514.
[32] Leznicki P, Roebuck Q P, Wunderley L, et al. The association of BAG6 with SGTA and tail-anchored proteins. PLoS One, 2013, 8(3): 59590-59598.
[33] Barbara A F, Shinichi Takayama, John C Reed. BAG-1L protein enhances androgen receptor function. J Biol Chem, 1998, 271(8): 11660-11666.
[34] Achenbach J, Nierhaus K H. The mechanics of ribosomal translocation. Biochimie, 2014, 10(1): 1016-1026.
[35] Jules Deforges, Nicolas Locker, Bruno Sargueil. mRNAs that specifically interact with eukaryotic ribosomal subunits. Biochimie, 2014, 12(8): 1-10.
[36] Hinnebusch A G. eIF3: a versatile scaffold for translation initiation complexes. Trends Biochem Sci, 2006, 31(10): 553-562.
[37] Sulistio Y A, Heese K. The Ubiquitin-proteasome system and molecular chaperone deregulation in Alzheimer's disease. Mol Neurobiol, 2015, 14(4): 1-27.
[38] Anne H P, Eric A J. The ubiquitin proteasome system in glia and its role in neurodegenerative diseases. Front Mol Neurosci, 2014, 7(2): 7301-7314.
[39] Liu H Y, Wang Z M, Chen J, et al. Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function. The Journal of Biological Chemistry, 2000, 275(30): 235-241.
[40] Carra S, Seguin S J, Landry J. HspB8 and Bag3: A new chaperone complex targeting misfolded proteins to macroautophagy. Autophagy, 2014, 4(2): 237-239.
[41] Turco M C, Rosati A, Graziano V, et al. BAG3 a multifaceted protein that regulates major cell pathways. Cell Death and Disease, 2011, 24(2): 1-6.
[42] Behl Christian. BAG3 and friends: co-chaperones in selective autophagy during aging and disease. Autophagy, 2011, 7(7): 795-798.
[43] Hishiya A, Salman M N, Carra S, et al. BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity. PLoS One, 2011, 6(3): e16828.
|
