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Article ; Online: Hexim1, an RNA-controlled protein hub.

Michels, Annemieke A / Bensaude, Olivier

2018 Volume 9, Issue 4, Page(s) 262–271

Abstract: Hexim1 acts as a tumor suppressor and is involved in the regulation of innate immunity. It was initially described as a non-coding RNA-dependent regulator of transcription. Here, we detail how 7SK RNA binds to Hexim1 and turns it into an inhibitor of the ...

Abstract	Hexim1 acts as a tumor suppressor and is involved in the regulation of innate immunity. It was initially described as a non-coding RNA-dependent regulator of transcription. Here, we detail how 7SK RNA binds to Hexim1 and turns it into an inhibitor of the positive transcription elongation factor (P-TEFb). In addition to its action on P-TEFb, it plays a role in a variety of different mechanisms: it controls the stability of transcription factor components and assists binding of transcription factors to their targets.
MeSH term(s)	Humans ; Immunity, Innate ; RNA, Long Noncoding/genetics ; RNA, Long Noncoding/metabolism ; RNA-Binding Proteins/immunology ; RNA-Binding Proteins/metabolism ; Transcription, Genetic/drug effects ; Transcription, Genetic/genetics
Chemical Substances	HEXIM1 protein, human ; RNA, Long Noncoding ; RNA-Binding Proteins ; long non-coding RNA 7SK, human
Language	English
Publishing date	2018-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2646974-1
ISSN	2154-1272 ; 2154-1264
ISSN (online)	2154-1272
ISSN	2154-1264
DOI	10.1080/21541264.2018.1429836
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Article ; Online: MAF1: a new target of mTORC1.

Michels, Annemieke A

Biochemical Society transactions

2011 Volume 39, Issue 2, Page(s) 487–491

Abstract: Yeast and mammalian MAF1 are both regulated by the TOR (target of rapamycin) pathway. However, the exact mechanisms of regulation diverge at TOR, with yeast Maf1 phosphorylated mainly by the TORC1 (TOR complex 1) substrate Sch9 kinase and mammalian MAF1 ... ...

Abstract	Yeast and mammalian MAF1 are both regulated by the TOR (target of rapamycin) pathway. However, the exact mechanisms of regulation diverge at TOR, with yeast Maf1 phosphorylated mainly by the TORC1 (TOR complex 1) substrate Sch9 kinase and mammalian MAF1 by mTORC1 (mammalian target of rapamycin complex 1) itself. Sch9 phosphorylation of yeast Maf1 regulates Maf1 localization, but it is less clear whether phosphorylation of human MAF1 regulates its localization. Replacement of phosphosites with alanine decreases Pol III (RNA polymerase III) transcription, but the effect is much more pronounced for human MAF1 than for the yeast protein. In both cases, Pol III repression can be further increased by rapamycin treatment or, in mammalian cells, serum starvation, suggesting that the TOR pathway controls another aspect of Pol III transcription that is closely linked to MAF1, as it depends on the presence of MAF1.
MeSH term(s)	Animals ; Catalytic Domain ; Humans ; Mechanistic Target of Rapamycin Complex 1 ; Models, Biological ; Multiprotein Complexes ; Phosphorylation ; Protein Transport ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Serine-Threonine Kinases/physiology ; Proteins/metabolism ; Proteins/physiology ; Repressor Proteins/chemistry ; Repressor Proteins/metabolism ; Repressor Proteins/physiology ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/physiology ; TOR Serine-Threonine Kinases ; Yeasts/genetics ; Yeasts/metabolism
Chemical Substances	MAF1 protein, human ; Multiprotein Complexes ; Proteins ; Repressor Proteins ; Saccharomyces cerevisiae Proteins ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; SCH9 protein, S cerevisiae (EC 2.7.11.1)
Language	English
Publishing date	2011-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0390487
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Article ; Online: An alternative D. melanogaster 7SK snRNP.

Nguyen, Duy / Buisine, Nicolas / Fayol, Olivier / Michels, Annemieke A / Bensaude, Olivier / Price, David H / Uguen, Patricia

BMC molecular and cell biology

2021 Volume 22, Issue 1, Page(s) 43

Abstract: Background: The 7SK small nuclear RNA (snRNA) found in most metazoans is a key regulator of P-TEFb which in turn regulates RNA polymerase II elongation. Although its primary sequence varies in protostomes, its secondary structure and function are ... ...

Abstract	Background: The 7SK small nuclear RNA (snRNA) found in most metazoans is a key regulator of P-TEFb which in turn regulates RNA polymerase II elongation. Although its primary sequence varies in protostomes, its secondary structure and function are conserved across evolutionary distant taxa. Results: Here, we describe a novel ncRNA sharing many features characteristic of 7SK RNAs, in D. melanogaster. We examined the structure of the corresponding gene and determined the expression profiles of the encoded RNA, called snRNA:7SK:94F, during development. It is probably produced from the transcription of a lncRNA which is processed into a mature snRNA. We also addressed its biological function and we show that, like dm7SK, this alternative 7SK interacts in vivo with the different partners of the P-TEFb complex, i.e. HEXIM, LARP7 and Cyclin T. This novel RNA is widely expressed across tissues. Conclusion: We propose that two distinct 7SK genes might contribute to the formation of the 7SK snRNP complex in D. melanogaster.
MeSH term(s)	Animals ; Cyclin T/metabolism ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Positive Transcriptional Elongation Factor B/genetics ; Positive Transcriptional Elongation Factor B/metabolism ; Protein Binding ; RNA, Long Noncoding/genetics ; RNA, Long Noncoding/metabolism ; RNA, Small Nuclear/genetics ; RNA, Small Nuclear/metabolism ; RNA-Binding Proteins/metabolism ; Ribonucleoproteins/metabolism ; Ribonucleoproteins, Small Nuclear/metabolism ; Transcription Factors
Chemical Substances	CycT protein, Drosophila ; Cyclin T ; Drosophila Proteins ; HEXIM protein, Drosophila ; LARP7 protein, Drosophila ; RNA, Long Noncoding ; RNA, Small Nuclear ; RNA-Binding Proteins ; Ribonucleoproteins ; Ribonucleoproteins, Small Nuclear ; Transcription Factors ; Positive Transcriptional Elongation Factor B (EC 2.7.11.-)
Language	English
Publishing date	2021-08-31
Publishing country	England
Document type	Journal Article
ISSN	2661-8850
ISSN (online)	2661-8850
DOI	10.1186/s12860-021-00381-7
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Article ; Online: RNA-driven cyclin-dependent kinase regulation: when CDK9/cyclin T subunits of P-TEFb meet their ribonucleoprotein partners.

Michels, Annemieke A / Bensaude, Olivier

Biotechnology journal

2008 Volume 3, Issue 8, Page(s) 1022–1032

Abstract: The positive transcription elongation factor (P-TEFb) consists of CDK9, a cyclin-dependent kinase and its cyclin T partner. It is required for transcription of most class II genes. Its activity is regulated by non-coding RNAs. The 7SK cellular RNA turns ... ...

Abstract	The positive transcription elongation factor (P-TEFb) consists of CDK9, a cyclin-dependent kinase and its cyclin T partner. It is required for transcription of most class II genes. Its activity is regulated by non-coding RNAs. The 7SK cellular RNA turns the HEXIM cellular protein into a P-TEFb inhibitor that binds its cyclin T subunit. Thus, P-TEFb activity responds to variations in global cellular transcriptional activity and to physiological conditions linked to cell differentiation, proliferation or cardiac hypertrophy. In contrast, the Tat activation region RNA plays an activating role. This feature at the 5' end of the human immunodeficiency (HIV) viral transcript associates with the viral protein Tat that in turn binds cyclin T1 and recruits active P-TEFb to the HIV promoter. This results in enhanced P-TEFb activity, which is critical for an efficient production of viral transcripts. Although discovered recently, the regulation of P-TEFb becomes a paradigm for non-coding RNAs that regulate transcription factors. It is also a unique example of RNA-driven regulation of a cyclindependent kinase.
MeSH term(s)	Cyclin-Dependent Kinase 9/chemistry ; Cyclin-Dependent Kinase 9/metabolism ; Cyclins/chemistry ; Cyclins/metabolism ; Gene Expression Regulation, Enzymologic/physiology ; Positive Transcriptional Elongation Factor B/chemistry ; Positive Transcriptional Elongation Factor B/metabolism ; Protein Subunits ; RNA/chemistry ; RNA/metabolism ; Ribonucleoproteins/chemistry ; Ribonucleoproteins/metabolism ; Structure-Activity Relationship
Chemical Substances	Cyclins ; Protein Subunits ; Ribonucleoproteins ; RNA (63231-63-0) ; Positive Transcriptional Elongation Factor B (EC 2.7.11.-) ; Cyclin-Dependent Kinase 9 (EC 2.7.11.22)
Language	English
Publishing date	2008-08
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2221885-3
ISSN	1860-7314 ; 1860-6768
ISSN (online)	1860-7314
ISSN	1860-6768
DOI	10.1002/biot.200800104
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Zs.A 6349: Show issues

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Article: Does Pol I talk to Pol II? Coordination of RNA polymerases in ribosome biogenesis.

Michels, Annemieke A / Hernandez, Nouria

Genes & development

2006 Volume 20, Issue 15, Page(s) 1982–1985

MeSH term(s)	RNA Polymerase I/physiology ; RNA Polymerase II/physiology ; RNA, Ribosomal, 5S/metabolism ; Ribosomes/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism
Chemical Substances	RNA, Ribosomal, 5S ; RNA Polymerase II (EC 2.7.7.-) ; RNA Polymerase I (EC 2.7.7.6)
Language	English
Publishing date	2006-08-01
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.1460706
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Zs.A 2292: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Phosphorylation by casein kinase 2 facilitates rRNA gene transcription by promoting dissociation of TIF-IA from elongating RNA polymerase I.

Bierhoff, Holger / Dundr, Miroslav / Michels, Annemieke A / Grummt, Ingrid

Molecular and cellular biology

2008 Volume 28, Issue 16, Page(s) 4988–4998

Abstract: The protein kinase casein kinase 2 (CK2) phosphorylates different components of the RNA polymerase I (Pol I) transcription machinery and exerts a positive effect on rRNA gene (rDNA) transcription. Here we show that CK2 phosphorylates the transcription ... ...

Abstract	The protein kinase casein kinase 2 (CK2) phosphorylates different components of the RNA polymerase I (Pol I) transcription machinery and exerts a positive effect on rRNA gene (rDNA) transcription. Here we show that CK2 phosphorylates the transcription initiation factor TIF-IA at serines 170 and 172 (Ser170/172), and this phosphorylation triggers the release of TIF-IA from Pol I after transcription initiation. Inhibition of Ser170/172 phosphorylation or covalent tethering of TIF-IA to the RPA43 subunit of Pol I inhibits rDNA transcription, leading to perturbation of nucleolar structure and cell cycle arrest. Fluorescence recovery after photobleaching and chromatin immunoprecipitation experiments demonstrate that dissociation of TIF-IA from Pol I is a prerequisite for proper transcription elongation. In support of phosphorylation of TIF-IA switching from the initiation into the elongation phase, dephosphorylation of Ser170/172 by FCP1 facilitates the reassociation of TIF-IA with Pol I, allowing a new round of rDNA transcription. The results reveal a mechanism by which the functional interplay between CK2 and FCP1 sustains multiple rounds of Pol I transcription.
MeSH term(s)	Amino Acid Sequence ; Animals ; Casein Kinase II/metabolism ; Cell Cycle ; Cell Nucleolus/metabolism ; Cell Proliferation ; DNA, Ribosomal/genetics ; Humans ; Mice ; Models, Biological ; Molecular Sequence Data ; NIH 3T3 Cells ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Pol1 Transcription Initiation Complex Proteins ; Promoter Regions, Genetic/genetics ; Protein Binding ; RNA Polymerase I/metabolism ; RNA Precursors/biosynthesis ; RNA, Ribosomal/genetics ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; Transcription, Genetic
Chemical Substances	DNA, Ribosomal ; Pol1 Transcription Initiation Complex Proteins ; RNA Precursors ; RNA, Ribosomal ; RRN3 protein, human ; Transcription Factors ; Phosphoserine (17885-08-4) ; Casein Kinase II (EC 2.7.11.1) ; RNA Polymerase I (EC 2.7.7.6) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; carboxy-terminal domain phosphatase (EC 3.1.3.16)
Language	English
Publishing date	2008-06-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00492-08
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Zs.A 1666: Show issues

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Article: Immunosuppressive therapy after solid-organ transplantation: does the INTERMED identify patients at risk of poor adherence?

Michaud, Laurent / Ludwig, Gundula / Berney, Sylvie / Rodrigues, Stéphanie / Niquille, Anne / Santschi, Valérie / Favre, Anne-Sophie / Lange, Anne-Catherine / Michels, Annemieke A / Vrijens, Bernard / Bugnon, Olivier / Pilon, Nathalie / Pascual, Manuel / Venetz, Jean-Pierre / Stiefel, Friedrich / Schneider, Marie-Paule

Pharmacy practice

2016 Volume 14, Issue 4, Page(s) 822

Abstract: Background: Lack of adherence to medication is a trigger of graft rejection in solid-organ transplant (SOT) recipients.: Objective: This exploratory study aimed to assess whether a biopsychosocial evaluation using the INTERMED instrument before ... ...

Abstract	Background: Lack of adherence to medication is a trigger of graft rejection in solid-organ transplant (SOT) recipients. Objective: This exploratory study aimed to assess whether a biopsychosocial evaluation using the INTERMED instrument before transplantation could identify SOT recipients at risk of suboptimal post-transplantation adherence to immunosuppressant drugs. We hypothesized that complex patients (INTERMED>20) might have lower medication adherence than noncomplex patients (INTERMED≤20). Methods: Each patient eligible for transplantation at the University Hospital of Lausanne, Switzerland, has to undergo a pre-transplantation psychiatric evaluation. In this context the patient was asked to participate in our study. The INTERMED was completed pre-transplantation, and adherence to immunosuppressive medication was monitored post-transplantation by electronic monitors for 12 months. The main outcome measure was the implementation and persistence to two calcineurin inhibitors, cyclosporine and tacrolimus, according to the dichotomized INTERMED score (>20 or ≤20). Results: Among the 50 SOT recipients who completed the INTERMED, 32 entered the study. The complex (N=11) and noncomplex patients (N=21) were similar in terms of age, sex and transplanted organ. Implementation was 94.2% in noncomplex patients versus 87.8% in complex patients (non-significant p-value). Five patients were lost to follow-up: one was non-persistent, and four refused electronic monitoring. Of the four patients who refused monitoring, two were complex and withdrew early, and two were noncomplex and withdrew later in the study. Conclusion: Patients identified as complex pre-transplant by the INTERMED tended to deviate from their immunosuppressant regimen, but the findings were not statistically significant. Larger studies are needed to evaluate this association further, as well as the appropriateness of using a nonspecific biopsychosocial instrument such as INTERMED in highly morbid patients who have complex social and psychological characteristics.
Language	English
Publishing date	2016-12-15
Publishing country	Spain
Document type	Journal Article
ZDB-ID	2414565-8
ISSN	1886-3655 ; 1885-642X
ISSN (online)	1886-3655
ISSN	1885-642X
DOI	10.18549/PharmPract.2016.04.822
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Article ; Online: mTORC1 directly phosphorylates and regulates human MAF1.

Michels, Annemieke A / Robitaille, Aaron M / Buczynski-Ruchonnet, Diane / Hodroj, Wassim / Reina, Jaime H / Hall, Michael N / Hernandez, Nouria

Molecular and cellular biology

2010 Volume 30, Issue 15, Page(s) 3749–3757

Abstract: mTORC1 is a central regulator of growth in response to nutrient availability, but few direct targets have been identified. RNA polymerase (pol) III produces a number of essential RNA molecules involved in protein synthesis, RNA maturation, and other ... ...

Abstract	mTORC1 is a central regulator of growth in response to nutrient availability, but few direct targets have been identified. RNA polymerase (pol) III produces a number of essential RNA molecules involved in protein synthesis, RNA maturation, and other processes. Its activity is highly regulated, and deregulation can lead to cell transformation. The human phosphoprotein MAF1 becomes dephosphorylated and represses pol III transcription after various stresses, but neither the significance of the phosphorylations nor the kinase involved is known. We find that human MAF1 is absolutely required for pol III repression in response to serum starvation or TORC1 inhibition by rapamycin or Torin1. The protein is phosphorylated mainly on residues S60, S68, and S75, and this inhibits its pol III repression function. The responsible kinase is mTORC1, which phosphorylates MAF1 directly. Our results describe molecular mechanisms by which mTORC1 controls human MAF1, a key repressor of RNA polymerase III transcription, and add a new branch to the signal transduction cascade immediately downstream of TORC1.
MeSH term(s)	Humans ; Phosphorylation ; RNA Polymerase III/antagonists & inhibitors ; RNA Polymerase III/genetics ; RNA Polymerase III/metabolism ; Signal Transduction/drug effects ; Signal Transduction/genetics ; Sirolimus/metabolism ; Sirolimus/pharmacology ; Transfection
Chemical Substances	RNA Polymerase III (EC 2.7.7.6) ; Sirolimus (W36ZG6FT64)
Language	English
Publishing date	2010-06-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00319-10
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Zs.A 1666: Show issues

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Article ; Online: Ubiquitination of HEXIM1 by HDM2.

Lau, Joanne / Lew, Qiao Jing / Diribarne, Gaelle / Michels, Annemieke A / Dey, Anwesha / Bensaude, Olivier / Lane, David P / Chao, Sheng-Hao

Cell cycle (Georgetown, Tex.)

2009 Volume 8, Issue 14, Page(s) 2247–2254

Abstract: Hexamethylene bis-acetamide inducible protein 1 (HEXIM1) is an inhibitor of the positive transcription elongation factor b (P-TEFb), which controls RNA polymerase II transcription and human immunodeficiency virus Tat transactivation. In cells, more than ... ...

Abstract	Hexamethylene bis-acetamide inducible protein 1 (HEXIM1) is an inhibitor of the positive transcription elongation factor b (P-TEFb), which controls RNA polymerase II transcription and human immunodeficiency virus Tat transactivation. In cells, more than half of P-TEFb is associated with HEXIM1 resulting in the inactivation of P-TEFb. Recently, we found that nucleophosmin (NPM), a key factor involved in p53 signaling pathway, interacts with HEXIM1 and activates P-TEFb-dependent transcription. Here we report that human double minute-2 protein (HDM2), a p53-specific E3 ubiquitin ligase, specifically ubiquitinates HEXIM1 through the lysine residues located within the basic region of HEXIM1. However, the HDM2-induced HEXIM1 ubiquitination does not lead to proteasome-mediated protein degradation. Fusion of ubiquitin to HEXIM1 demonstrates stronger inhibition on P-TEFb-dependent transcription. Our results demonstrate that HDM2 functions as a specific E3 ubiquitin ligase for HEXIM1, suggesting a possible role for HEXIM1 ubiquitination in the regulation of P-TEFb activity.
MeSH term(s)	Cell Line ; Cysteine Proteinase Inhibitors/pharmacology ; Humans ; Leupeptins/pharmacology ; Nuclear Proteins/metabolism ; Positive Transcriptional Elongation Factor B/genetics ; Positive Transcriptional Elongation Factor B/metabolism ; Proto-Oncogene Proteins c-mdm2/metabolism ; RNA-Binding Proteins/metabolism ; Signal Transduction ; Tumor Suppressor Protein p53/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Cysteine Proteinase Inhibitors ; HEXIM1 protein, human ; Leupeptins ; Nuclear Proteins ; RNA-Binding Proteins ; Tumor Suppressor Protein p53 ; nucleophosmin (117896-08-9) ; MDM2 protein, human (EC 2.3.2.27) ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Positive Transcriptional Elongation Factor B (EC 2.7.11.-) ; benzyloxycarbonylleucyl-leucyl-leucine aldehyde (RF1P63GW3K)
Language	English
Publishing date	2009-08-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.8.14.9015
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Zs.A 5881: Show issues

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Article ; Online: Inhibition of Tat activity by the HEXIM1 protein

Majello Barbara / Michels Annemieke A / Napolitano Giuliana / Varrone Francesca / Fraldi Alessandro / Bensaude Olivier / Lania Luigi

Retrovirology, Vol 2, Iss 1, p

2005 Volume 42

Abstract: Abstract Background The positive transcription elongation factor b (P-TEFb) composed by CDK9/CyclinT1 subunits is a dedicated co-factor of HIV transcriptional transactivator Tat protein. Transcription driven by the long terminal repeat (LTR) of HIV ... ...

Abstract	Abstract Background The positive transcription elongation factor b (P-TEFb) composed by CDK9/CyclinT1 subunits is a dedicated co-factor of HIV transcriptional transactivator Tat protein. Transcription driven by the long terminal repeat (LTR) of HIV involves formation of a quaternary complex between P-TEFb, Tat and the TAR element. This recruitment is necessary to enhance the processivity of RNA Pol II from the HIV-1 5' LTR promoter. The activity of P-TEFb is regulated in vivo and in vitro by the HEXIM1/7SK snRNA ribonucleic-protein complex. Results Here we report that Tat transactivation is effectively inhibited by co-expression of HEXIM1 or its paralog HEXIM2. HEXIM1 expression specifically represses transcription mediated by the direct activation of P-TEFb through artificial recruitment of GAL4-CycT1. Using appropriate HEXIM1 mutants we determined that effective Tat-inhibition entails the 7SK snRNA basic recognition motif as well as the C-terminus region required for interaction with cyclin T1. Enhanced expression of HEXIM1 protein modestly affects P-TEFb activity, suggesting that HEXIM1-mediated repression of Tat activity is not due to a global inhibition of cellular transcription. Conclusion These results point to a pivotal role of P-TEFb for Tat's optimal transcription activity and suggest that cellular proteins that regulate P-TEFb activity might exert profound effects on Tat function in vivo .
Keywords	Medicine (General) ; R5-920 ; Medicine ; R ; DOAJ:Medicine (General) ; DOAJ:Health Sciences ; Immunologic diseases. Allergy ; RC581-607
Subject code	570 ; 571
Language	English
Publishing date	2005-07-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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