SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages. Berger SB, Romero X, Ma C, Wang G, Faubion WA, Liao G, Compeer E, Keszei M, Rameh L, Wang N, Boes M, Regueiro JR, Reinecker HC, Terhorst C (2010) Nat Immunol 11: 920-7 ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Ye J, Rawson RB, Komuro R, Chen X, Davé UP, Prywes R, Brown MS, Goldstein JL (2000) Mol Cell 6: 1355-64 Heat shock proteins in cancer: chaperones of tumorigenesis. Calderwood SK, Khaleque MA, Sawyer DB, Ciocca DR (2006) Trends Biochem Sci 31: 164-72 In and out: histone variant exchange in chromatin. Jin J, Cai Y, Li B, Conaway RC, Workman JL, Conaway JW, Kusch T (2005) Trends Biochem Sci 30: 680-7 Endoplasmic reticulum stress in the pathogenesis of fibrotic disease. Kropski JA, Blackwell TS (2018) J Clin Invest 128: 64-73 Emerging anticancer therapeutic targets and the cardiovascular system: is there cause for concern? Peng X, Pentassuglia L, Sawyer DB (2010) Circ Res 106: 1022-34 The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo. Riggs DL, Roberts PJ, Chirillo SC, Cheung-Flynn J, Prapapanich V, Ratajczak T, Gaber R, Picard D, Smith DF (2003) EMBO J 22: 1158-67 Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex. Matsuura H, Kirschner AN, Longnecker R, Jardetzky TS (2010) Proc Natl Acad Sci U S A 107: 22641-6 Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation. Tranguch S, Cheung-Flynn J, Daikoku T, Prapapanich V, Cox MB, Xie H, Wang H, Das SK, Smith DF, Dey SK (2005) Proc Natl Acad Sci U S A 102: 14326-31 Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis. Salghetti SE, Muratani M, Wijnen H, Futcher B, Tansey WP (2000) Proc Natl Acad Sci U S A 97: 3118-23 Tapasin: an ER chaperone that controls MHC class I assembly with peptide. Grandea AG, Van Kaer L (2001) Trends Immunol 22: 194-9 Molecular evidence for increased expression of genes related to immune and chaperone function in the prefrontal cortex in schizophrenia. Arion D, Unger T, Lewis DA, Levitt P, Mirnics K (2007) Biol Psychiatry 62: 711-21 The ubiquitin-selective chaperone Cdc48/p97 associates with Ubx3 to modulate monoubiquitylation of histone H2B. Bonizec M, Hérissant L, Pokrzywa W, Geng F, Wenzel S, Howard GC, Rodriguez P, Krause S, Tansey WP, Hoppe T, Dargemont C (2014) Nucleic Acids Res 42: 10975-86 Intrarenal distribution of clusterin following reduction of renal mass. Correa-Rotter R, Hostetter TH, Manivel JC, Eddy AA, Rosenberg ME (1992) Kidney Int 41: 938-50 Localization of clusterin in the epimembranous deposits of passive Heymann nephritis. Eddy AA, Fritz IB (1991) Kidney Int 39: 247-52 The novel chemical entity YTR107 inhibits recruitment of nucleophosmin to sites of DNA damage, suppressing repair of DNA double-strand breaks and enhancing radiosensitization. Sekhar KR, Reddy YT, Reddy PN, Crooks PA, Venkateswaran A, McDonald WH, Geng L, Sasi S, Van Der Waal RP, Roti JL, Salleng KJ, Rachakonda G, Freeman ML (2011) Clin Cancer Res 17: 6490-9 Functional specificity of co-chaperone interactions with Hsp90 client proteins. Riggs DL, Cox MB, Cheung-Flynn J, Prapapanich V, Carrigan PE, Smith DF (2004) Crit Rev Biochem Mol Biol 39: 279-95 Functional roles of TAP and tapasin in the assembly of M3-N-formylated peptide complexes. Chun T, Grandea AG, Lybarger L, Forman J, Van Kaer L, Wang CR (2001) J Immunol 167: 1507-14 Subunit 1 of the prefoldin chaperone complex is required for lymphocyte development and function. Cao S, Carlesso G, Osipovich AB, Llanes J, Lin Q, Hoek KL, Khan WN, Ruley HE (2008) J Immunol 181: 476-84 The reaper-binding protein scythe modulates apoptosis and proliferation during mammalian development. Desmots F, Russell HR, Lee Y, Boyd K, McKinnon PJ (2005) Mol Cell Biol 25: 10329-37 On the path to the heat shock response: destabilization and formation of partially folded protein intermediates, a consequence of protein thiol modification. Freeman ML, Borrelli MJ, Meredith MJ, Lepock JR (1999) Free Radic Biol Med 26: 737-45 Binding-site interactions between Epstein-Barr virus fusion proteins gp42 and gH/gL reveal a peptide that inhibits both epithelial and B-cell membrane fusion. Kirschner AN, Lowrey AS, Longnecker R, Jardetzky TS (2007) J Virol 81: 9216-29 Use of gHgL for attachment of Epstein-Barr virus to epithelial cells compromises infection. Borza CM, Morgan AJ, Turk SM, Hutt-Fletcher LM (2004) J Virol 78: 5007-14 Epstein-Barr virus gH is essential for penetration of B cells but also plays a role in attachment of virus to epithelial cells. Molesworth SJ, Lake CM, Borza CM, Turk SM, Hutt-Fletcher LM (2000) J Virol 74: 6324-32 Mutations of Epstein-Barr virus gH that are differentially able to support fusion with B cells or epithelial cells. Wu L, Borza CM, Hutt-Fletcher LM (2005) J Virol 79: 10923-30 HIV-1 Resistance to the Capsid-Targeting Inhibitor PF74 Results in Altered Dependence on Host Factors Required for Virus Nuclear Entry. Zhou J, Price AJ, Halambage UD, James LC, Aiken C (2015) J Virol 89: 9068-79 Molecular chaperone interactions with steroid receptors: an update. Cheung J, Smith DF (2000) Mol Endocrinol 14: 939-46 Physiological role for the cochaperone FKBP52 in androgen receptor signaling. Cheung-Flynn J, Prapapanich V, Cox MB, Riggs DL, Suarez-Quian C, Smith DF (2005) Mol Endocrinol 19: 1654-66 Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function. Schultz-Norton JR, McDonald WH, Yates JR, Nardulli AM (2006) Mol Endocrinol 20: 1982-95 Loss of αB-crystallin function in zebrafish reveals critical roles in the development of the lens and stress resistance of the heart. Mishra S, Wu SY, Fuller AW, Wang Z, Rose KL, Schey KL, Mchaourab HS (2018) J Biol Chem 293: 740-753 Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding. Ishikawa Y, Vranka JA, Boudko SP, Pokidysheva E, Mizuno K, Zientek K, Keene DR, Rashmir-Raven AM, Nagata K, Winand NJ, Bächinger HP (2012) J Biol Chem 287: 22253-65 Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. Sondermann H, Ho AK, Listenberger LL, Siegers K, Moarefi I, Wente SR, Hartl FU, Young JC (2002) J Biol Chem 277: 33220-7 A lymphocyte-specific Ltk tyrosine kinase isoform is retained in the endoplasmic reticulum in association with calnexin. Snijders AJ, Ho SC, Haase VH, Pillai S, Bernards A (1997) J Biol Chem 272: 1297-301 Defining the interaction of the protease CpaA with its type II secretion chaperone CpaB and its contribution to virulence in species. Kinsella RL, Lopez J, Palmer LD, Salinas ND, Skaar EP, Tolia NH, Feldman MF (2017) J Biol Chem 292: 19628-19638 The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Ho AK, Raczniak GA, Ives EB, Wente SR (1998) Mol Biol Cell 9: 355-73 Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo. Xiao J, Kim LS, Graham TR (2006) Mol Biol Cell 17: 3281-90 Interaction of Gcn4 with target gene chromatin is modulated by proteasome function. Howard GC, Tansey WP (2016) Mol Biol Cell 27: 2735-41 Anticholinergic drugs rescue synaptic plasticity in DYT1 dystonia: role of M1 muscarinic receptors. Maltese M, Martella G, Madeo G, Fagiolo I, Tassone A, Ponterio G, Sciamanna G, Burbaud P, Conn PJ, Bonsi P, Pisani A (2014) Mov Disord 29: 1655-65 Immunocytochemical localization and determination of hormone-induced synthesis of the sulfated oviductal glycoproteins. Oliphant G, Reynolds AB, Smith PF, Ross PR, Marta JS (1984) Biol Reprod 31: 165-74 Depletion of the C. elegans NAC engages the unfolded protein response, resulting in increased chaperone expression and apoptosis. Arsenovic PT, Maldonado AT, Colleluori VD, Bloss TA (2012) PLoS One 7: e44038
Hints: (1) double-click or double-tap to navigate to a node. (2) Grab a node and move it to arrange the graph.