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Article ; Online: ARTISTRY-7: phase III trial of nemvaleukin alfa plus pembrolizumab vs chemotherapy for platinum-resistant ovarian cancer.

2023 Volume 19, Issue 23, Page(s) 1577–1591

Abstract: Standard single-agent nonplatinum chemotherapy provides only modest benefit in a small proportion of patients with platinum-resistant/-refractory ovarian cancer, with objective response rates of 6-20% and progression-free survival of ≈3-4 months. ... ...

Abstract	Standard single-agent nonplatinum chemotherapy provides only modest benefit in a small proportion of patients with platinum-resistant/-refractory ovarian cancer, with objective response rates of 6-20% and progression-free survival of ≈3-4 months. Nemvaleukin alfa (nemvaleukin, ALKS 4230) is a novel cytokine designed to capture and expand the therapeutic potential of high-dose interleukin-2 (IL-2) while mitigating its associated toxicity issues. Nemvaleukin preferentially activates cytotoxic CD8
MeSH term(s)	Humans ; Female ; Ovarian Neoplasms ; CD8-Positive T-Lymphocytes ; Carcinoma, Ovarian Epithelial/drug therapy ; Carcinoma, Ovarian Epithelial/etiology ; Antibodies, Monoclonal, Humanized/therapeutic use ; Enzyme Inhibitors/therapeutic use ; Adjuvants, Immunologic/therapeutic use ; Antineoplastic Combined Chemotherapy Protocols/adverse effects ; Clinical Trials, Phase III as Topic
Chemical Substances	pembrolizumab (DPT0O3T46P) ; Antibodies, Monoclonal, Humanized ; Enzyme Inhibitors ; Adjuvants, Immunologic
Language	English
Publishing date	2023-06-19
Publishing country	England
Document type	Journal Article ; Clinical Trial Protocol
ZDB-ID	2274956-1
ISSN	1744-8301 ; 1479-6694
ISSN (online)	1744-8301
ISSN	1479-6694
DOI	10.2217/fon-2023-0246
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Article ; Online: Heat shock proteins: cell protection through protein triage.

Lanneau, David / Wettstein, Guillaume / Bonniaud, Philippe / Garrido, Carmen

TheScientificWorldJournal

2010 Volume 10, Page(s) 1543–1552

Abstract: Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A ...

Abstract	Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A coordinated interaction between the HSPs (renaturation) and the proteasome (degradation) must exist to assure protein quality control mechanisms. Although it still remains unknown how the decision of folding vs. degradation is taken, many pieces of evidence demonstrate that HSPs interact directly or indirectly with the proteasome, assuring quite selectively the proteasomal degradation of certain proteins under stress conditions. In this review, we will describe the different data that demonstrate a role for HSP90, HSP70, HSP27, and áB-crystallin in the partitioning of proteins to either one of these pathways, referred as protein triage.
MeSH term(s)	Animals ; Crystallins/metabolism ; HSP27 Heat-Shock Proteins/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Models, Biological ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Signal Transduction
Chemical Substances	Crystallins ; HSP27 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2010-08-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2075968-X
ISSN	1537-744X ; 1537-744X
ISSN (online)	1537-744X
ISSN	1537-744X
DOI	10.1100/tsw.2010.152
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Article ; Online: Heat Shock Proteins

David Lanneau / Guillaume Wettstein / Philippe Bonniaud / Carmen Garrido

The Scientific World Journal, Vol 10, Pp 1543-

Cell Protection through Protein Triage

2010 Volume 1552

Abstract	Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A coordinated interaction between the HSPs (renaturation) and the proteasome (degradation) must exist to assure protein quality control mechanisms. Although it still remains unknown how the decision of folding vs. degradation is taken, many pieces of evidence demonstrate that HSPs interact directly or indirectly with the proteasome, assuring quite selectively the proteasomal degradation of certain proteins under stress conditions. In this review, we will describe the different data that demonstrate a role for HSP90, HSP70, HSP27, and alpha-B-crystallin in the partitioning of proteins to either one of these pathways, referred as protein triage.
Keywords	Technology ; T ; Medicine ; R ; Science ; Q
Language	English
Publishing date	2010-01-01T00:00:00Z
Publisher	Hindawi Limited
Document type	Article ; Online
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Article ; Online: Apoptosis versus cell differentiation: role of heat shock proteins HSP90, HSP70 and HSP27.

Lanneau, David / de Thonel, Aurelie / Maurel, Sebastien / Didelot, Celine / Garrido, Carmen

Prion

2007 Volume 1, Issue 1, Page(s) 53–60

Abstract: Heat shock proteins HSP27, HSP70 and HSP90 are molecular chaperones whose expression is increased after many different types of stress. They have a protective function helping the cell to cope with lethal conditions. The cytoprotective function of HSPs ... ...

Abstract	Heat shock proteins HSP27, HSP70 and HSP90 are molecular chaperones whose expression is increased after many different types of stress. They have a protective function helping the cell to cope with lethal conditions. The cytoprotective function of HSPs is largely explained by their anti-apoptotic function. HSPs have been shown to interact with different key apoptotic proteins. As a result, HSPs can block essentially all apoptotic pathways, most of them involving the activation of cystein proteases called caspases. Apoptosis and differentiation are physiological processes that share many common features, for instance, chromatin condensation and the activation of caspases are frequently observed. It is, therefore, not surprising that many recent reports imply HSPs in the differentiation process. This review will comment on the role of HSP90, HSP70 and HSP27 in apoptosis and cell differentiation. HSPs may determine de fate of the cells by orchestrating the decision of apoptosis versus differentiation.
MeSH term(s)	Animals ; Apoptosis/physiology ; Caspases/metabolism ; Cell Differentiation/physiology ; Chromatin/metabolism ; HSP27 Heat-Shock Proteins/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans
Chemical Substances	Chromatin ; HSP27 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins ; Caspases (EC 3.4.22.-)
Language	English
Publishing date	2007-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2267671-5
ISSN	1933-690X ; 1933-690X
ISSN (online)	1933-690X
ISSN	1933-690X
DOI	10.4161/pri.1.1.4059
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Article: Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins.

Didelot, Celine / Lanneau, David / Brunet, Mathilde / Joly, Anne-Laure / De Thonel, Aurelie / Chiosis, Gabriela / Garrido, Carmen

Current medicinal chemistry

2007 Volume 14, Issue 27, Page(s) 2839–2847

Abstract: Stress or heat shock proteins (Hsps) Hsp90, Hsp70 and Hsp27 are chaperones that assist the proteins in their folding, stability, assembly into multi-protein complexes and transport across cellular membranes. The expression of some of them is highly ... ...

Abstract	Stress or heat shock proteins (Hsps) Hsp90, Hsp70 and Hsp27 are chaperones that assist the proteins in their folding, stability, assembly into multi-protein complexes and transport across cellular membranes. The expression of some of them is highly induced in response to a wide variety of physiological and environmental insults. Hsps have a dual function depending on their intracellular or extracellular location. Intracellular Hsps have a protective function. They allow the cells to survive to lethal conditions. The cytoprotective functions of Hsps can largely explain by their anti-apoptotic properties. Hsp90, Hsp70 and Hsp27 can directly interact with different proteins of the tightly regulated programmed cell death machinery and thereby block the apoptotic process at distinct key points. In cancer cells, where the expression of Hsp27, Hsp70 and/or Hsp90 is frequently abnormally high, they participate in oncogenesis and in resistance to chemotherapy. Therefore, the inhibition of Hsps has become an interesting strategy in cancer therapy. In contrast to intracellular Hsps, extracellular located or membrane-bound Hsps mediate immunological functions. They can elicit an immune response modulated either by the adaptive or innate immune system. In cancer, most immunotherapeutical approaches based on extracellular Hsps exploit their carrier function for immunogenic peptides. This review will discuss this different and often paradoxical approaches in cancer therapy based on the dual role of Hsps, protective/tumorigenic versus immunogenic.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Drug Screening Assays, Antitumor ; Heat-Shock Proteins/antagonists & inhibitors ; Humans ; Neoplasms/drug therapy ; Tumor Cells, Cultured
Chemical Substances	Antineoplastic Agents ; Heat-Shock Proteins
Language	English
Publishing date	2007-01-11
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1319315-6
ISSN	1875-533X ; 0929-8673
ISSN (online)	1875-533X
ISSN	0929-8673
DOI	10.2174/092986707782360079
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Article ; Online: Peptides and aptamers targeting HSP70: a novel approach for anticancer chemotherapy.

Rérole, Anne-Laure / Gobbo, Jessica / De Thonel, Aurelie / Schmitt, Elise / Pais de Barros, Jean Paul / Hammann, Arlette / Lanneau, David / Fourmaux, Eric / Demidov, Oleg N / Deminov, Oleg / Micheau, Olivier / Lagrost, Laurent / Colas, Pierre / Kroemer, Guido / Garrido, Carmen

Cancer research

2011 Volume 71, Issue 2, Page(s) 484–495

Abstract: The inhibition of heat shock protein 70 (HSP70) is an emerging strategy in cancer therapy. Unfortunately, no specific inhibitors are clinically available. By yeast two-hybrid screening, we have identified multiple peptide aptamers that bind HSP70. When ... ...

Abstract	The inhibition of heat shock protein 70 (HSP70) is an emerging strategy in cancer therapy. Unfortunately, no specific inhibitors are clinically available. By yeast two-hybrid screening, we have identified multiple peptide aptamers that bind HSP70. When expressed in human tumor cells, two among these peptide aptamers-A8 and A17-which bind to the peptide-binding and the ATP-binding domains of HSP70, respectively, specifically inhibited the chaperone activity, thereby increasing the cells' sensitivity to apoptosis induced by anticancer drugs. The 13-amino acid peptide from the variable region of A17 (called P17) retained the ability to specifically inhibit HSP70 and induced the regression of subcutaneous tumors in vivo after local or systemic injection. This antitumor effect was associated with an important recruitment of macrophages and T lymphocytes into the tumor bed. Altogether, these data indicate that peptide aptamers or peptides that target HSP70 may be considered as novel lead compounds for cancer therapy.
MeSH term(s)	Animals ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Apoptosis/drug effects ; Aptamers, Peptide/chemistry ; Aptamers, Peptide/genetics ; Aptamers, Peptide/pharmacology ; HSP70 Heat-Shock Proteins/antagonists & inhibitors ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; HeLa Cells ; Humans ; Melanoma, Experimental/drug therapy ; Mice ; Mice, Inbred C57BL ; Molecular Targeted Therapy/methods ; Peptides/chemistry ; Peptides/genetics ; Peptides/pharmacology ; Protein Structure, Tertiary ; Rats ; Transfection
Chemical Substances	Antineoplastic Agents ; Aptamers, Peptide ; HSP70 Heat-Shock Proteins ; Peptides
Language	English
Publishing date	2011-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-10-1443
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Article ; Online: HSP27 controls GATA-1 protein level during erythroid cell differentiation.

de Thonel, Aurelie / Vandekerckhove, Julie / Lanneau, David / Selvakumar, Subramaniam / Courtois, Geneviève / Hazoume, Adonis / Brunet, Mathilde / Maurel, Sebastien / Hammann, Arlette / Ribeil, Jean Antoine / Zermati, Yael / Gabet, Anne Sophie / Boyes, Joan / Solary, Eric / Hermine, Olivier / Garrido, Carmen

Blood

2010 Volume 116, Issue 1, Page(s) 85–96

Abstract: Heat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific ... ...

Abstract	Heat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific proteins. Here, we show that globin transcription factor 1 (GATA-1) is a client protein of HSP27. In 2 models of erythroid differentiation; that is, in the human erythroleukemia cell line, K562 induced to differentiate into erythroid cells on hemin exposure and CD34(+) human cells ex vivo driven to erythroid differentiation in liquid culture, depletion of HSP27 provokes an accumulation of GATA-1 and impairs terminal maturation. More specifically, we demonstrate that, in the late stages of the erythroid differentiation program, HSP27 is phosphorylated in a p38-dependent manner, enters the nucleus, binds to GATA-1, and induces its ubiquitination and proteasomal degradation, provided that the transcription factor is acetylated. We conclude that HSP27 plays a role in the fine-tuning of terminal erythroid differentiation through regulation of GATA-1 content and activity.
MeSH term(s)	Animals ; Antigens, CD34/blood ; COS Cells ; Cell Differentiation ; Cell Nucleus/metabolism ; Cells, Cultured ; Chlorocebus aethiops ; Erythroid Cells/cytology ; Erythroid Cells/drug effects ; Erythroid Cells/metabolism ; GATA1 Transcription Factor/genetics ; GATA1 Transcription Factor/metabolism ; HSP27 Heat-Shock Proteins/genetics ; HSP27 Heat-Shock Proteins/metabolism ; HeLa Cells ; Heat-Shock Proteins ; Humans ; Imidazoles/pharmacology ; Immunoblotting ; Interleukin-6/pharmacology ; K562 Cells ; Leupeptins/pharmacology ; Molecular Chaperones ; Phosphorylation/drug effects ; Proteasome Endopeptidase Complex/metabolism ; Proteasome Inhibitors ; Protein Binding ; Pyridines/pharmacology ; RNA Interference ; Transforming Growth Factor beta/pharmacology ; Ubiquitination/drug effects ; p38 Mitogen-Activated Protein Kinases/antagonists & inhibitors ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Antigens, CD34 ; GATA1 Transcription Factor ; GATA1 protein, human ; HSP27 Heat-Shock Proteins ; HSPB1 protein, human ; Heat-Shock Proteins ; Imidazoles ; Interleukin-6 ; Leupeptins ; Molecular Chaperones ; Proteasome Inhibitors ; Pyridines ; Transforming Growth Factor beta ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; SB 203580 (OU13V1EYWQ) ; benzyloxycarbonylleucyl-leucyl-leucine aldehyde (RF1P63GW3K)
Language	English
Publishing date	2010-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2009-09-241778
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Article ; Online: Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells.

The Journal of clinical investigation

2010 Volume 120, Issue 2, Page(s) 457–471

Abstract: Myeloid-derived suppressor cells (MDSCs) have been identified in humans and mice as a population of immature myeloid cells with the ability to suppress T cell activation. They accumulate in tumor-bearing mice and humans and have been shown to contribute ... ...

Abstract	Myeloid-derived suppressor cells (MDSCs) have been identified in humans and mice as a population of immature myeloid cells with the ability to suppress T cell activation. They accumulate in tumor-bearing mice and humans and have been shown to contribute to cancer development. Here, we have isolated tumor-derived exosomes (TDEs) from mouse cell lines and shown that an interaction between TDE-associated Hsp72 and MDSCs determines the suppressive activity of the MDSCs via activation of Stat3. In addition, tumor-derived soluble factors triggered MDSC expansion via activation of Erk. TDE-associated Hsp72 triggered Stat3 activation in MDSCs in a TLR2/MyD88-dependent manner through autocrine production of IL-6. Importantly, decreasing exosome production using dimethyl amiloride enhanced the in vivo antitumor efficacy of the chemotherapeutic drug cyclophosphamide in 3 different mouse tumor models. We also demonstrated that this mechanism is relevant in cancer patients, as TDEs from a human tumor cell line activated human MDSCs and triggered their suppressive function in an Hsp72/TLR2-dependent manner. Further, MDSCs from cancer patients treated with amiloride, a drug used to treat high blood pressure that also inhibits exosome formation, exhibited reduced suppressor functions. Collectively, our findings show in both mice and humans that Hsp72 expressed at the surface of TDEs restrains tumor immune surveillance by promoting MDSC suppressive functions.
MeSH term(s)	Amiloride/pharmacology ; Amiloride/therapeutic use ; Animals ; Cell Line ; Cell Line, Tumor ; Cyclophosphamide/therapeutic use ; Exosomes/drug effects ; Exosomes/immunology ; Exosomes/physiology ; HSP72 Heat-Shock Proteins/physiology ; Humans ; Immunosuppression ; Mice ; Mice, Nude ; Neoplasms/drug therapy ; Neoplasms/immunology ; T-Lymphocytes/immunology ; T-Lymphocytes, Regulatory/immunology
Chemical Substances	HSP72 Heat-Shock Proteins ; Amiloride (7DZO8EB0Z3) ; Cyclophosphamide (8N3DW7272P)
Language	English
Publishing date	2010-01-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI40483
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Article: SSR180711, a novel selective alpha7 nicotinic receptor partial agonist: (1) binding and functional profile.

Biton, Bruno / Bergis, Olivier E / Galli, Frédéric / Nedelec, Alain / Lochead, Alistair W / Jegham, Samir / Godet, Danielle / Lanneau, Christophe / Santamaria, Raphaël / Chesney, Françoise / Léonardon, Jacques / Granger, Patrick / Debono, Marc W / Bohme, Georg A / Sgard, Frédéric / Besnard, François / Graham, David / Coste, Annick / Oblin, André /

Curet, Olivier / Vigé, Xavier / Voltz, Corinne / Rouquier, Liliane / Souilhac, Josiane / Santucci, Vincent / Gueudet, Christiane / Françon, Dominique / Steinberg, Régis / Griebel, Guy / Oury-Donat, Florence / George, Pascal / Avenet, Patrick / Scatton, Bernard

Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology

2007 Volume 32, Issue 1, Page(s) 1–16

Abstract: In this paper, we report on the pharmacological and functional profile of SSR180711 (1,4-Diazabicyclo[3.2.2]nonane-4-carboxylic acid, 4-bromophenyl ester), a new selective alpha7 acetylcholine nicotinic receptor (n-AChRs) partial agonist. SSR180711 ... ...

Abstract	In this paper, we report on the pharmacological and functional profile of SSR180711 (1,4-Diazabicyclo[3.2.2]nonane-4-carboxylic acid, 4-bromophenyl ester), a new selective alpha7 acetylcholine nicotinic receptor (n-AChRs) partial agonist. SSR180711 displays high affinity for rat and human alpha7 n-AChRs (K(i) of 22+/-4 and 14+/-1 nM, respectively). Ex vivo (3)[H]alpha-bungarotoxin binding experiments demonstrate that SSR180711 rapidly penetrates into the brain (ID(50)=8 mg/kg p.o.). In functional studies performed with human alpha7 n-AChRs expressed in Xenopus oocytes or GH4C1 cells, the compound shows partial agonist effects (intrinsic activity=51 and 36%, EC(50)=4.4 and 0.9 microM, respectively). In rat cultured hippocampal neurons, SSR180711 induced large GABA-mediated inhibitory postsynaptic currents and small alpha-bungarotoxin sensitive currents through the activation of presynaptic and somato-dendritic alpha7 n-AChRs, respectively. In mouse hippocampal slices, the compound increased the amplitude of both glutamatergic (EPSCs) and GABAergic (IPSCs) postsynaptic currents evoked in CA1 pyramidal cells. In rat and mouse hippocampal slices, a concentration of 0.3 muM of SSR180711 increased long-term potentiation (LTP) in the CA1 field. Null mutation of the alpha7 n-AChR gene totally abolished SSR180711-induced modulation of EPSCs, IPSCs and LTP in mice. Intravenous administration of SSR180711 strongly increased the firing rate of single ventral pallidum neurons, extracellularly recorded in anesthetized rats. In microdialysis experiments, administration of the compound (3-10 mg/kg i.p.) dose-dependently increased extracellular acetylcholine (ACh) levels in the hippocampus and prefrontal cortex of freely moving rats. Together, these results demonstrate that SSR180711 is a selective and partial agonist at human, rat and mouse alpha7 n-AChRs, increasing glutamatergic neurotransmission, ACh release and LTP in the hippocampus.
MeSH term(s)	Animals ; Animals, Newborn ; Binding Sites/drug effects ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology ; Cells, Cultured ; Dose-Response Relationship, Drug ; Drug Interactions ; Gene Expression/drug effects ; Gene Expression/physiology ; Hippocampus/cytology ; Humans ; In Vitro Techniques ; Membrane Potentials/drug effects ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurons/drug effects ; Neurons/physiology ; Nicotinic Agonists/chemistry ; Nicotinic Agonists/pharmacokinetics ; Nicotinic Agonists/pharmacology ; Nicotinic Antagonists/pharmacology ; Oocytes/physiology ; Patch-Clamp Techniques/methods ; Protein Subunits/drug effects ; Protein Subunits/physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, Nicotinic/deficiency ; Receptors, Nicotinic/physiology ; Synaptic Transmission/drug effects ; Synaptic Transmission/physiology ; alpha7 Nicotinic Acetylcholine Receptor ; gamma-Aminobutyric Acid/pharmacology
Chemical Substances	Bridged Bicyclo Compounds, Heterocyclic ; Chrna7 protein, human ; Chrna7 protein, mouse ; Chrna7 protein, rat ; Nicotinic Agonists ; Nicotinic Antagonists ; Protein Subunits ; Receptors, Nicotinic ; SSR180711 ; alpha7 Nicotinic Acetylcholine Receptor ; gamma-Aminobutyric Acid (56-12-2)
Language	English
Publishing date	2007-01
Publishing country	England
Document type	Journal Article
ZDB-ID	639471-1
ISSN	1740-634X ; 0893-133X
ISSN (online)	1740-634X
ISSN	0893-133X
DOI	10.1038/sj.npp.1301189
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