Hop (タンパク質)
関連文献

“Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes”. Electrophoresis 13 (12):  960–9. (December 1992). doi:10.1002/elps.11501301199. PMID 1286667.
“Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1”. The Journal of Biological Chemistry 267 (12):  8485–91. (April 1992). doi:10.1016/S0021-9258(18)42471-4. PMID 1569099.
“Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene 138 (1–2):  171–4. (January 1994). doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
“Normalization and subtraction: two approaches to facilitate gene discovery”. Genome Research 6 (9):  791–806. (September 1996). doi:10.1101/gr.6.9.791. PMID 8889548.
“Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation”. The Journal of Biological Chemistry 272 (20):  13047–54. (May 1997). doi:10.1074/jbc.272.20.13047. PMID 9148915.
“Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70”. The Journal of Biological Chemistry 272 (34):  21213–20. (August 1997). doi:10.1074/jbc.272.34.21213. PMID 9261129.
“Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library”. Gene 200 (1–2):  149–56. (October 1997). doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
“Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1”. Cell 94 (4):  471–80. (August 1998). doi:10.1016/S0092-8674(00)81588-3. PMID 9727490.
“Antigens recognized by autologous antibody in patients with renal-cell carcinoma”. International Journal of Cancer 83 (4):  456–64. (November 1999). doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479.
“Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine”. Cell 101 (2):  199–210. (April 2000). doi:10.1016/S0092-8674(00)80830-2. PMID 10786835.
“HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor”. The Journal of Biological Chemistry 277 (14):  11873–81. (April 2002). doi:10.1074/jbc.M111445200. PMID 11809754.
“Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes”. The Journal of Biological Chemistry 277 (22):  19265–75. (May 2002). doi:10.1074/jbc.M109002200. PMID 11877417.
“Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection”. The EMBO Journal 21 (13):  3307–16. (July 2002). doi:10.1093/emboj/cdf325. PMC 125391. PMID 12093732. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC125391/.
“The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex”. The Journal of Biological Chemistry 277 (41):  38294–304. (October 2002). doi:10.1074/jbc.M206566200. PMID 12161444.
“The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically”. Biological Chemistry 383 (9):  1335–42. (September 2002). doi:10.1515/BC.2002.152. PMID 12437126.
“A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death”. The Journal of Biological Chemistry 278 (51):  51901–10. (December 2003). doi:10.1074/jbc.M309655200. PMID 14532270.
“Nuclear translocation of the Hsp70/Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases”. Journal of Cell Science 117 (Pt 5):  701–10. (February 2004). doi:10.1242/jcs.00905. PMID 14754904.
“Immunoaffinity profiling of tyrosine phosphorylation in cancer cells”. Nature Biotechnology 23 (1):  94–101. (January 2005). doi:10.1038/nbt1046. PMID 15592455.