HSPBP1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Hsp70-binding protein 1''' is a [[protein]] that in humans is encoded by the ''HSPBP1'' [[gene]].<ref name="pmid10786638">{{cite journal | vauthors = Raynes DA, Guerriero V | title = Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70 | journal = Biochimica et Biophysica Acta | volume = 1490 | issue = 1-2 | pages = 203–7 | date = Jan 2000 | pmid = 10786638 | pmc =  | doi = 10.1016/s0167-4781(99)00238-9 }}</ref><ref name="pmid9830037">{{cite journal | vauthors = Raynes DA, Guerriero V | title = Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein | journal = The Journal of Biological Chemistry | volume = 273 | issue = 49 | pages = 32883–8 | date = Dec 1998 | pmid = 9830037 | pmc = | doi = 10.1074/jbc.273.49.32883 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSPBP1 hsp70-interacting protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23640| accessdate = }}</ref>
| update_page = yes
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_HSPBP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xqr.
| PDB = {{PDB2|1xqr}}, {{PDB2|1xqs}}
| Name = Hsp70-interacting protein
| HGNCid = 
| Symbol = HSPBP1
| AltSymbols =;
| OMIM = 
| ECnumber = 
| Homologene = 40827
| MGIid = 1913495
| GeneAtlas_image1 = PBB_GE_HSPBP1_202415_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004857 |text = enzyme inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23640
    | Hs_Ensembl = ENSG00000133265
    | Hs_RefseqProtein = XP_001128038
    | Hs_RefseqmRNA = XM_001128038
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 60465411
    | Hs_GenLoc_end = 60483540
    | Hs_Uniprot = Q9NZL4
    | Mm_EntrezGene = 66245
    | Mm_Ensembl = ENSMUSG00000063802
    | Mm_RefseqmRNA = NM_024172
    | Mm_RefseqProtein = NP_077134
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 4263608
    | Mm_GenLoc_end = 4288050
    | Mm_Uniprot = Q99P31
  }}
}}
'''Hsp70-interacting protein''', also known as '''HSPBP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSPBP1 hsp70-interacting protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23640| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
HSPBP1 has been shown to [[Protein-protein interaction|interact]] with [[HSPA8]]<ref name=pmid16189514>{{cite journal|authorlink30=Huda Zoghbi | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}</ref><ref name=pmid16169070>{{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = Sep 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}</ref> and [[HSPA4]].<ref name=pmid14503850>{{cite journal | vauthors = Oh WK, Song J | title = Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation | journal = Molecules and Cells | volume = 16 | issue = 1 | pages = 84–91 | date = Aug 2003 | pmid = 14503850 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R | title = Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1 | journal = Cell | volume = 94 | issue = 4 | pages = 471–80 | date = Aug 1998 | pmid = 9727490 | doi = 10.1016/S0092-8674(00)81588-3 }}
| citations =
* {{cite journal | vauthors = Kabani M, McLellan C, Raynes DA, Guerriero V, Brodsky JL | title = HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor | journal = FEBS Letters | volume = 531 | issue = 2 | pages = 339–42 | date = Nov 2002 | pmid = 12417338 | doi = 10.1016/S0014-5793(02)03570-6 }}
*{{cite journal | author=Zou J, Guo Y, Guettouche T, ''et al.'' |title=Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. |journal=Cell |volume=94 |issue= 4 |pages= 471-80 |year= 1998 |pmid= 9727490 |doi= }}
* {{cite journal | vauthors = McLellan CA, Raynes DA, Guerriero V | title = HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain | journal = The Journal of Biological Chemistry | volume = 278 | issue = 21 | pages = 19017–22 | date = May 2003 | pmid = 12651857 | doi = 10.1074/jbc.M301109200 }}
*{{cite journal  | author=Raynes DA, Guerriero V |title=Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32883-8 |year= 1999 |pmid= 9830037 |doi=  }}
* {{cite journal | vauthors = Oh WK, Song J | title = Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation | journal = Molecules and Cells | volume = 16 | issue = 1 | pages = 84–91 | date = Aug 2003 | pmid = 14503850 | doi =  }}
*{{cite journal  | author=Raynes DA, Guerriero V |title=Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70. |journal=Biochim. Biophys. Acta |volume=1490 |issue= 1-2 |pages= 203-7 |year= 2000 |pmid= 10786638 |doi=  }}
* {{cite journal | vauthors = Lu QF, Bai M, Zhang HJ, Li JC, Xiao CF, Chen S, Wu TC | title = [Co-detection of P21, P53 and HSP70 and their possible role in diagnosis of polycyclic aromatic hydrocarbons (PAHs)-related lung cancer] | journal = Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi = Zhonghua Laodong Weisheng Zhiyebing Zazhi = Chinese Journal of Industrial Hygiene and Occupational Diseases | volume = 21 | issue = 5 | pages = 359–61 | date = Oct 2003 | pmid = 14761400 | doi =  }}
*{{cite journal | author=Kabani M, McLellan C, Raynes DA, ''et al.'' |title=HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. |journal=FEBS Lett. |volume=531 |issue= 2 |pages= 339-42 |year= 2002 |pmid= 12417338 |doi= }}
* {{cite journal | vauthors = Alberti S, Böhse K, Arndt V, Schmitz A, Höhfeld J | title = The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator | journal = Molecular Biology of the Cell | volume = 15 | issue = 9 | pages = 4003–10 | date = Sep 2004 | pmid = 15215316 | pmc = 515335 | doi = 10.1091/mbc.E04-04-0293 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A | title = Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange | journal = Molecular Cell | volume = 17 | issue = 3 | pages = 367–79 | date = Feb 2005 | pmid = 15694338 | doi = 10.1016/j.molcel.2004.12.023 }}
*{{cite journal | author=McLellan CA, Raynes DA, Guerriero V |title=HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain. |journal=J. Biol. Chem. |volume=278 |issue= 21 |pages= 19017-22 |year= 2003 |pmid= 12651857 |doi= 10.1074/jbc.M301109200 }}
* {{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = Sep 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}
*{{cite journal | author=Oh WK, Song J |title=Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation. |journal=Mol. Cells |volume=16 |issue= 1 |pages= 84-91 |year= 2004 |pmid= 14503850 |doi=  }}
* {{cite journal | vauthors = Dai Q, Qian SB, Li HH, McDonough H, Borchers C, Huang D, Takayama S, Younger JM, Ren HY, Cyr DM, Patterson C | title = Regulation of the cytoplasmic quality control protein degradation pathway by BAG2 | journal = The Journal of Biological Chemistry | volume = 280 | issue = 46 | pages = 38673–81 | date = Nov 2005 | pmid = 16169850 | doi = 10.1074/jbc.M507986200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}
*{{cite journal  | author=Lu QF, Bai M, Zhang HJ, ''et al.'' |title=[Co-detection of P21, P53 and HSP70 and their possible role in diagnosis of polycyclic aromatic hydrocarbons (PAHs)-related lung cancer] |journal=Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi |volume=21 |issue= 5 |pages= 359-61 |year= 2004 |pmid= 14761400 |doi=  }}
* {{cite journal | vauthors = Gottwald E, Herschbach M, Lahni B, Miesfeld RL, Kunz S, Raynes DA, Guerriero V | title = Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression | journal = Cell Biology International | volume = 30 | issue = 6 | pages = 553–8 | date = Jun 2006 | pmid = 16677834 | doi = 10.1016/j.cellbi.2006.03.005 }}
*{{cite journal | author=Alberti S, Böhse K, Arndt V, ''et al.'' |title=The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. |journal=Mol. Biol. Cell |volume=15 |issue= 9 |pages= 4003-10 |year= 2005 |pmid= 15215316 |doi= 10.1091/mbc.E04-04-0293 }}
* {{cite journal | vauthors = Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY | title = A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration | journal = Cell | volume = 125 | issue = 4 | pages = 801–14 | date = May 2006 | pmid = 16713569 | doi = 10.1016/j.cell.2006.03.032 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Bivik C, Rosdahl I, Ollinger K | title = Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes | journal = Carcinogenesis | volume = 28 | issue = 3 | pages = 537–44 | date = Mar 2007 | pmid = 16950797 | doi = 10.1093/carcin/bgl152 }}
*{{cite journal  | author=Shomura Y, Dragovic Z, Chang HC, ''et al.'' |title=Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. |journal=Mol. Cell |volume=17 |issue= 3 |pages= 367-79 |year= 2005 |pmid= 15694338 |doi= 10.1016/j.molcel.2004.12.023 }}
* {{cite journal | vauthors = Swayne LA, Braun JE | title = Aggregate-centered redistribution of proteins by mutant huntingtin | journal = Biochemical and Biophysical Research Communications | volume = 354 | issue = 1 | pages = 39–44 | date = Mar 2007 | pmid = 17208201 | doi = 10.1016/j.bbrc.2006.12.129 }}
*{{cite journal | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal | author=Dai Q, Qian SB, Li HH, ''et al.'' |title=Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. |journal=J. Biol. Chem. |volume=280 |issue= 46 |pages= 38673-81 |year= 2006 |pmid= 16169850 |doi= 10.1074/jbc.M507986200 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Otsuki T, Ota T, Nishikawa T, ''et al.'' |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117-26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal  | author=Gottwald E, Herschbach M, Lahni B, ''et al.'' |title=Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression. |journal=Cell Biol. Int. |volume=30 |issue= 6 |pages= 553-8 |year= 2006 |pmid= 16677834 |doi= 10.1016/j.cellbi.2006.03.005 }}
*{{cite journal | author=Lim J, Hao T, Shaw C, ''et al.'' |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801-14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal | author=Bivik C, Rosdahl I, Ollinger K |title=Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes. |journal=Carcinogenesis |volume=28 |issue= 3 |pages= 537-44 |year= 2007 |pmid= 16950797 |doi= 10.1093/carcin/bgl152 }}
*{{cite journal | author=Swayne LA, Braun JE |title=Aggregate-centered redistribution of proteins by mutant huntingtin. |journal=Biochem. Biophys. Res. Commun. |volume=354 |issue= 1 |pages= 39-44 |year= 2007 |pmid= 17208201 |doi= 10.1016/j.bbrc.2006.12.129 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=23640}}
{{WikiDoc Sources}}
 
 
{{gene-19-stub}}
 
[[Category:Armadillo-repeat-containing proteins]]

Latest revision as of 02:09, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Hsp70-binding protein 1 is a protein that in humans is encoded by the HSPBP1 gene.[1][2][3]

Interactions

HSPBP1 has been shown to interact with HSPA8[4][5] and HSPA4.[6]

References

  1. ↑ Raynes DA, Guerriero V (Jan 2000). "Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70". Biochimica et Biophysica Acta. 1490 (1–2): 203–7. doi:10.1016/s0167-4781(99)00238-9. PMID 10786638.
  2. ↑ Raynes DA, Guerriero V (Dec 1998). "Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein". The Journal of Biological Chemistry. 273 (49): 32883–8. doi:10.1074/jbc.273.49.32883. PMID 9830037.
  3. ↑ "Entrez Gene: HSPBP1 hsp70-interacting protein".
  4. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  5. ↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  6. ↑ Oh WK, Song J (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Molecules and Cells. 16 (1): 84–91. PMID 14503850.

Further reading

  • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (Aug 1998). "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. doi:10.1016/S0092-8674(00)81588-3. PMID 9727490.
  • Kabani M, McLellan C, Raynes DA, Guerriero V, Brodsky JL (Nov 2002). "HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor". FEBS Letters. 531 (2): 339–42. doi:10.1016/S0014-5793(02)03570-6. PMID 12417338.
  • McLellan CA, Raynes DA, Guerriero V (May 2003). "HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain". The Journal of Biological Chemistry. 278 (21): 19017–22. doi:10.1074/jbc.M301109200. PMID 12651857.
  • Oh WK, Song J (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Molecules and Cells. 16 (1): 84–91. PMID 14503850.
  • Lu QF, Bai M, Zhang HJ, Li JC, Xiao CF, Chen S, Wu TC (Oct 2003). "[Co-detection of P21, P53 and HSP70 and their possible role in diagnosis of polycyclic aromatic hydrocarbons (PAHs)-related lung cancer]". Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi = Zhonghua Laodong Weisheng Zhiyebing Zazhi = Chinese Journal of Industrial Hygiene and Occupational Diseases. 21 (5): 359–61. PMID 14761400.
  • Alberti S, Böhse K, Arndt V, Schmitz A, Höhfeld J (Sep 2004). "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator". Molecular Biology of the Cell. 15 (9): 4003–10. doi:10.1091/mbc.E04-04-0293. PMC 515335. PMID 15215316.
  • Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A (Feb 2005). "Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange". Molecular Cell. 17 (3): 367–79. doi:10.1016/j.molcel.2004.12.023. PMID 15694338.
  • Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  • Dai Q, Qian SB, Li HH, McDonough H, Borchers C, Huang D, Takayama S, Younger JM, Ren HY, Cyr DM, Patterson C (Nov 2005). "Regulation of the cytoplasmic quality control protein degradation pathway by BAG2". The Journal of Biological Chemistry. 280 (46): 38673–81. doi:10.1074/jbc.M507986200. PMID 16169850.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Gottwald E, Herschbach M, Lahni B, Miesfeld RL, Kunz S, Raynes DA, Guerriero V (Jun 2006). "Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression". Cell Biology International. 30 (6): 553–8. doi:10.1016/j.cellbi.2006.03.005. PMID 16677834.
  • Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
  • Bivik C, Rosdahl I, Ollinger K (Mar 2007). "Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes". Carcinogenesis. 28 (3): 537–44. doi:10.1093/carcin/bgl152. PMID 16950797.
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