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Article ; Online: New insights into SARS-CoV-2 Lumipulse G salivary antigen testing: accuracy, safety and short TAT enhance surveillance.

Aita, Ada / Navaglia, Filippo / Moz, Stefania / Contran, Nicole / Barbaro, Francesco / Cattelan, Anna Maria / Padoan, Andrea / Cosma, Chiara / Faggian, Diego / Plebani, Mario / Basso, Daniela

Clinical chemistry and laboratory medicine

2022 Volume 61, Issue 2, Page(s) 323–331

Abstract: ... TaqPath rRT-PCR) and chemiluminescent Ag assays (Lumipulse G). The effect of sample pre-treatment ...

Abstract	Objectives: The rapid, accurate and safe detection of SARS-CoV-2 is the key to improving surveillance and infection containment. The aim of the present study was to ascertain whether, after heat/chemical inactivation, SARS-CoV-2 N antigen chemiluminescence (CLEIA) assay in saliva remains a valid alternative to molecular testing. Methods: In 2022, 139 COVID-19 inpatients and 467 healthcare workers were enrolled. In 606 self-collected saliva samples (Salivette), SARS-CoV-2 was detected by molecular (TaqPath rRT-PCR) and chemiluminescent Ag assays (Lumipulse G). The effect of sample pre-treatment (extraction solution-ES or heating) on antigen recovery was verified. Results: Salivary SARS-CoV-2 antigen assay was highly accurate (AUC=0.959, 95% CI: 0.943-0.974), with 90% sensitivity and 92% specificity. Of the 254 antigen positive samples, 29 were false positives. We demonstrated that heterophilic antibodies could be a cause of false positive results. A significant antigen concentration decrease was observed after ES treatment (p=0.0026), with misclassification of 43 samples. Heat had a minimal impact, after treatment the correct classification of cases was maintained. Conclusions: CLEIA SARS-CoV-2 salivary antigen provides accurate, timely and high-throughput results that remain accurate also after heat inactivation, thus ensuring a safer work environment. This supports the use of salivary antigen detection by CLEIA in surveillance programs.
MeSH term(s)	Humans ; SARS-CoV-2 ; COVID-19/diagnosis ; COVID-19 Testing ; Saliva ; Sensitivity and Specificity
Language	English
Publishing date	2022-10-26
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1418007-8
ISSN	1437-4331 ; 1434-6621 ; 1437-8523
ISSN (online)	1437-4331
ISSN	1434-6621 ; 1437-8523
DOI	10.1515/cclm-2022-0849
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Article: Blurring Boundaries: Receptor Tyrosine Kinases as functional G Protein-Coupled Receptors.

Crudden, Caitrin / Shibano, Takashi / Song, Dawei / Suleymanova, Naida / Girnita, Ada / Girnita, Leonard

International review of cell and molecular biology

2018 Volume 339, Page(s) 1–40

Abstract: ... and other RTKs make direct use of the G protein-coupled receptor (GPCR) components G proteins, GRKs ...

Abstract	Receptor tyrosine kinases (RTKs) such as the insulin-like growth factor type 1 receptor (IGF-1R) control important biological activities as well as being involved in pathological processes. Due to their supportive nature in many human cancers they have long been considered attractive therapeutic targets. However, lessons learnt from early targeting trials highlight that a simple "active versus inactive" state model with classical kinase-only signaling is overly simplistic and does not describe reality. A vast amount of evidence exists disproving this model and hence provides a rational explanation for failure of many targeting agents designed under such a paradigm. In addition, substantial evidence exists that the IGF-1R and other RTKs make direct use of the G protein-coupled receptor (GPCR) components G proteins, GRKs, and β-arrestins, outside of their traditional receptor family frame. In this chapter we review the evidence that RTKs can undertake a wide range of active conformations, capable of distinct downstream signal cascades and propose an RTK/GPCR functional hybrid model, while discussing the implications of such an update on therapeutic drug development pipelines.
MeSH term(s)	Animals ; G-Protein-Coupled Receptor Kinases/metabolism ; Humans ; Neoplasms/metabolism ; Neoplasms/pathology ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptors, G-Protein-Coupled/metabolism ; Transcriptional Activation/genetics ; beta-Arrestins/metabolism
Chemical Substances	Receptors, G-Protein-Coupled ; beta-Arrestins ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; G-Protein-Coupled Receptor Kinases (EC 2.7.11.16)
Language	English
Publishing date	2018-04-03
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2427220-6
ISSN	1937-6448 ; 0074-7696
ISSN	1937-6448 ; 0074-7696
DOI	10.1016/bs.ircmb.2018.02.006
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Article ; Online: Inhibition of G Protein-Coupled Receptor Kinase 2 Promotes Unbiased Downregulation of IGF1 Receptor and Restrains Malignant Cell Growth.

Crudden, Caitrin / Shibano, Takashi / Song, Dawei / Dragomir, Mihnea P / Cismas, Sonia / Serly, Julianna / Nedelcu, Daniela / Fuentes-Mattei, Enrique / Tica, Andrei / Calin, George A / Girnita, Ada / Girnita, Leonard

Cancer research

2020 Volume 81, Issue 2, Page(s) 501–514

Abstract: ... cascades is termed biased signaling. Although comprehensively recognized for the G protein-coupled ...

Abstract	The ability of a receptor to preferentially activate only a subset of available downstream signal cascades is termed biased signaling. Although comprehensively recognized for the G protein-coupled receptors (GPCR), this process is scarcely explored downstream of receptor tyrosine kinases (RTK), including the cancer-relevant insulin-like growth factor-1 receptor (IGF1R). Successful IGF1R targeting requires receptor downregulation, yet therapy-mediated removal from the cell surface activates cancer-protective β-arrestin-biased signaling (β-arr-BS). As these overlapping processes are initiated by the β-arr/IGF1R interaction and controlled by GPCR-kinases (GRK), we explored GRKs as potential anticancer therapeutic targets to disconnect IGF1R downregulation and β-arr-BS. Transgenic modulation demonstrated that GRK2 inhibition or GRK6 overexpression enhanced degradation of IGF1R, but both scenarios sustained IGF1-induced β-arr-BS. Pharmacologic inhibition of GRK2 by the clinically approved antidepressant, serotonin reuptake inhibitor paroxetine (PX), recapitulated the effects of GRK2 silencing with dose- and time-dependent IGF1R downregulation without associated β-arr-BS.
MeSH term(s)	Animals ; Apoptosis ; Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Bone Neoplasms/genetics ; Bone Neoplasms/metabolism ; Bone Neoplasms/pathology ; Cell Proliferation ; G-Protein-Coupled Receptor Kinase 2/genetics ; G-Protein-Coupled Receptor Kinase 2/metabolism ; G-Protein-Coupled Receptor Kinases/genetics ; G-Protein-Coupled Receptor Kinases/metabolism ; Gene Expression Regulation, Neoplastic ; Humans ; Insulin-Like Growth Factor I/genetics ; Insulin-Like Growth Factor I/metabolism ; Male ; Mice ; Mice, Nude ; Phosphorylation ; Receptor, IGF Type 1/genetics ; Receptor, IGF Type 1/metabolism ; Sarcoma, Ewing/genetics ; Sarcoma, Ewing/metabolism ; Sarcoma, Ewing/pathology ; Tumor Cells, Cultured ; Ubiquitination ; Xenograft Model Antitumor Assays
Chemical Substances	Biomarkers, Tumor ; IGF1 protein, human ; IGF1R protein, human ; Insulin-Like Growth Factor I (67763-96-6) ; Receptor, IGF Type 1 (EC 2.7.10.1) ; GRK2 protein, human (EC 2.7.11.15) ; G-Protein-Coupled Receptor Kinase 2 (EC 2.7.11.16) ; G-Protein-Coupled Receptor Kinases (EC 2.7.11.16) ; G-protein-coupled receptor kinase 6 (EC 2.7.11.16)
Language	English
Publishing date	2020-11-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-20-1662
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Article: A novel thrombin binding aptamer containing a G-LNA residue.

Virno, Ada / Randazzo, Antonio / Giancola, Concetta / Bucci, Mariarosaria / Cirino, Giuseppe / Mayol, Luciano

Bioorganic & medicinal chemistry

2007 Volume 15, Issue 17, Page(s) 5710–5718

Abstract: ... properties of a new modified thrombin binding aptamer (TBA) containing a G-LNA residue, namely d(5' ... structure consisting of two G-tetrads connected by three edge-wise TT, TGT, and TT loops. d(5' ...

Abstract	In this work, we report the solution structure, thermodynamic studies, and the pharmacological properties of a new modified thrombin binding aptamer (TBA) containing a G-LNA residue, namely d(5'-GGTTGGTGTGGTTGg-3'), where upper case and lower case letters represent DNA and LNA residues, respectively. NMR and CD spectroscopy, as well as molecular dynamics and mechanic calculations, has been used to characterize the three-dimensional structure. The modified oligonucleotide is characterized by a chair-like structure consisting of two G-tetrads connected by three edge-wise TT, TGT, and TT loops. d(5'-GGTTGGTGTGGTTGg-3') is characterized by the same folding of TBA, being two strands parallel to each other and two strands oriented in opposite manner. This led to a syn-anti-syn-anti and anti-syn-anti-syn arrangements of the Gs in the two tetrads. d(5'-GGTTGGTGTGGTTGg-3') possesses an anticoagulant activity, even if decreased with respect to the TBA.
MeSH term(s)	Aptamers, Nucleotide/chemical synthesis ; Aptamers, Nucleotide/chemistry ; Aptamers, Nucleotide/pharmacology ; Circular Dichroism ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Conformation ; Nucleotides/chemical synthesis ; Nucleotides/chemistry ; Nucleotides/pharmacology ; Prothrombin/antagonists & inhibitors ; Prothrombin/metabolism ; Ribose/analogs & derivatives ; Ribose/chemical synthesis ; Ribose/chemistry ; Ribose/pharmacology ; Thermodilution
Chemical Substances	2'-O-4'-C-methylene-ribofuranosyl nucleotide ; Aptamers, Nucleotide ; Nucleotides ; thrombin aptamer (145563-68-4) ; Ribose (681HV46001) ; Prothrombin (9001-26-7)
Language	English
Publishing date	2007-09-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2007.06.008
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Book: Molecular characterization of PBAN G-protein coupled receptors in moth pest species

Rafaeli, Ada / Jurenka, Russell

design of antagonists

2013

Institution	United States-Israel Binational Agricultural Research and Development Fund
Author's details	Ada Rafaeli, Russell Jurenka
Keywords	Helicoverpa/Physiology. ; Peptide hormones/Receptors. ; Pheromones.
Language	English
Size	[7] p.
Publisher	BARD
Publishing place	Bet Dagan, Israel
Document type	Book
Note	Final report. ; Project no. IS-4163-08.
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Article ; Online: Selective recruitment of G protein-coupled receptor kinases (GRKs) controls signaling of the insulin-like growth factor 1 receptor.

Zheng, Huiyuan / Worrall, Claire / Shen, Hongchang / Issad, Tarik / Seregard, Stefan / Girnita, Ada / Girnita, Leonard

Proceedings of the National Academy of Sciences of the United States of America

2012 Volume 109, Issue 18, Page(s) 7055–7060

Abstract: β-Arrestins are multifunctional proteins that play central roles in G protein-coupled receptor ...

Abstract	β-Arrestins are multifunctional proteins that play central roles in G protein-coupled receptor (GPCR) trafficking and signaling. β-Arrestin1 is also recruited to the insulin-like growth factor-1 receptor (IGF-1R), a receptor tyrosine kinase (RTK), mediating receptor degradation and signaling. Because GPCR phosphorylation by GPCR-kinases (GRKs) governs interactions of the receptors with β-arrestins, we investigated the regulatory roles of the four widely expressed GRKs on IGF-1R signaling/degradation. By suppressing GRK expression with siRNA, we demonstrated that lowering GRK5/6 abolishes IGF1-mediated ERK and AKT activation, whereas GRK2 inhibition increases ERK activation and partially inhibits AKT signaling. Conversely, β-arrestin-mediated ERK signaling is enhanced by overexpression of GRK6 and diminished by GRK2. Similarly, we demonstrated opposing effects of GRK2 and -6 on IGF-1R degradation: GRK2 decreases whereas GRK6 enhances ligand-induced degradation. GRK2 and GRK6 coimmunoprecipitate with IGF-1R and increase IGF-1R serine phosphorylation, promoting β-arrestin1 association. Using immunoprecipitation, confocal microscopy, and FRET analysis, we demonstrated β-arrestin/IGF-1R association to be transient for GRK2 and stable for GRK6. Using bioinformatic studies we identified serines 1248 and 1291 as the major serine phosphorylation sites of the IGF-1R, and subsequent mutation analysis demonstrated clear effects on IGF-1R signaling and degradation, mirroring alterations by GRKs. Targeted mutation of S1248 recapitulates GRK2 modulation, whereas S1291 mutation resembles GRK6 effects on IGF-1R signaling/degradation, consistent with GRK isoform-specific serine phosphorylation. This study demonstrates distinct roles for GRK isoforms in IGF-1R signaling through β-arrestin binding with divergent functional outcomes.
MeSH term(s)	Amino Acid Sequence ; Animals ; Arrestins/metabolism ; Base Sequence ; Cell Line ; Fluorescence Resonance Energy Transfer ; G-Protein-Coupled Receptor Kinase 2/genetics ; G-Protein-Coupled Receptor Kinase 2/metabolism ; G-Protein-Coupled Receptor Kinases/antagonists & inhibitors ; G-Protein-Coupled Receptor Kinases/genetics ; G-Protein-Coupled Receptor Kinases/metabolism ; HEK293 Cells ; Humans ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; RNA, Small Interfering/genetics ; Receptor, IGF Type 1/chemistry ; Receptor, IGF Type 1/genetics ; Receptor, IGF Type 1/metabolism ; Serine/chemistry ; Signal Transduction ; Substrate Specificity ; beta-Arrestins
Chemical Substances	Arrestins ; RNA, Small Interfering ; beta-Arrestins ; Serine (452VLY9402) ; Receptor, IGF Type 1 (EC 2.7.10.1) ; GRK2 protein, human (EC 2.7.11.15) ; G-Protein-Coupled Receptor Kinase 2 (EC 2.7.11.16) ; G-Protein-Coupled Receptor Kinases (EC 2.7.11.16) ; G-protein-coupled receptor kinase 6 (EC 2.7.11.16)
Language	English
Publishing date	2012-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Validation Study
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1118359109
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Article: A further contribution to the extreme variability of quadruplex structures from oligodeoxyribonucleotides containing inversion of polarity sites in the G-tract.

Galeone, Aldo / Mayol, Luciano / Virgilio, Antonella / Virno, Ada / Randazzo, Antonio

Molecular bioSystems

2008 Volume 4, Issue 5, Page(s) 426–430

Abstract: Structural insight into DNA quadruplex structures formed by oligodeoxyribonucleotides 3'TG5'-5'GGGT3' (QS55) and 5'TG3'-3'GGGT5' (QS33) is presented. NMR analysis reveals that QS33 forms a parallel-like four-fold symmetric quadruplex, while QS55 ... ...

Abstract	Structural insight into DNA quadruplex structures formed by oligodeoxyribonucleotides 3'TG5'-5'GGGT3' (QS55) and 5'TG3'-3'GGGT5' (QS33) is presented. NMR analysis reveals that QS33 forms a parallel-like four-fold symmetric quadruplex, while QS55 possesses a two-fold symmetry and is characterized by a tetrameric antiparallel quadruplex embedded between two parallel tracts. The results reported here describe unprecedented quadruplex complexes provided by peculiar structural features never reported to date. These structures might inspire the design of new aptameric nucleic acids characterized by novel structural motifs hardly realizable with unmodified DNA/RNA.
MeSH term(s)	Circular Dichroism ; G-Quadruplexes ; Genetic Variation ; Magnetic Resonance Spectroscopy ; Oligodeoxyribonucleotides/chemistry ; Temperature
Chemical Substances	Oligodeoxyribonucleotides
Language	English
Publishing date	2008-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2188635-0
ISSN	1742-2051 ; 1742-206X
ISSN (online)	1742-2051
ISSN	1742-206X
DOI	10.1039/b718778e
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Article: Selective recruitment of G protein-coupled receptor kinases (GRKs) controls signaling of the insulin-like growth factor 1 receptor

Zheng, Huiyuan / Worrall, Claire / Shen, Hongchang / Issad, Tarik / Seregard, Stefan / Girnita, Ada / Girnita, Leonard

Proceedings of the National Academy of Sciences of the United States of America. 2012 May 1, v. 109, no. 18

2012

Abstract: β-Arrestins are multifunctional proteins that play central roles in G protein-coupled receptor ...

Abstract	β-Arrestins are multifunctional proteins that play central roles in G protein-coupled receptor (GPCR) trafficking and signaling. β-Arrestin1 is also recruited to the insulin-like growth factor-1 receptor (IGF-1R), a receptor tyrosine kinase (RTK), mediating receptor degradation and signaling. Because GPCR phosphorylation by GPCR-kinases (GRKs) governs interactions of the receptors with β-arrestins, we investigated the regulatory roles of the four widely expressed GRKs on IGF-1R signaling/degradation. By suppressing GRK expression with siRNA, we demonstrated that lowering GRK5/6 abolishes IGF1-mediated ERK and AKT activation, whereas GRK2 inhibition increases ERK activation and partially inhibits AKT signaling. Conversely, β-arrestin–mediated ERK signaling is enhanced by overexpression of GRK6 and diminished by GRK2. Similarly, we demonstrated opposing effects of GRK2 and -6 on IGF-1R degradation: GRK2 decreases whereas GRK6 enhances ligand-induced degradation. GRK2 and GRK6 coimmunoprecipitate with IGF-1R and increase IGF-1R serine phosphorylation, promoting β-arrestin1 association. Using immunoprecipitation, confocal microscopy, and FRET analysis, we demonstrated β-arrestin/IGF-1R association to be transient for GRK2 and stable for GRK6. Using bioinformatic studies we identified serines 1248 and 1291 as the major serine phosphorylation sites of the IGF-1R, and subsequent mutation analysis demonstrated clear effects on IGF-1R signaling and degradation, mirroring alterations by GRKs. Targeted mutation of S1248 recapitulates GRK2 modulation, whereas S1291 mutation resembles GRK6 effects on IGF-1R signaling/degradation, consistent with GRK isoform-specific serine phosphorylation. This study demonstrates distinct roles for GRK isoforms in IGF-1R signaling through β-arrestin binding with divergent functional outcomes.
Keywords	bioinformatics ; insulin-like growth factor I ; microscopy ; mitogen-activated protein kinase ; mutation ; phosphorylation ; proteins ; receptors ; serine ; small interfering RNA ; tyrosine
Language	English
Dates of publication	2012-0501
Size	p. 7055-7060.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1118359109
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Article: 23S rRNA 2058A-->G alteration mediates ketolide resistance in combination with deletion in L22.

Berisio, Rita / Corti, Natascia / Pfister, Peter / Yonath, Ada / Böttger, Erik C

Antimicrobial agents and chemotherapy

2006 Volume 50, Issue 11, Page(s) 3816–3823

Abstract: Resistance to macrolides and ketolides occurs mainly via alterations in RNA moieties of the drug-binding site. Using an A2058G mutant of Mycobacterium smegmatis, additional telithromycin resistance was acquired via deletion of 15 residues from protein ... ...

Abstract	Resistance to macrolides and ketolides occurs mainly via alterations in RNA moieties of the drug-binding site. Using an A2058G mutant of Mycobacterium smegmatis, additional telithromycin resistance was acquired via deletion of 15 residues from protein L22. Molecular modeling, based on the crystal structure of the large ribosomal subunit from Deinococcus radiodurans complexed with telithromycin, shows that the telithromycin carbamate group is located in the proximity of the tip of the L22 hairpin-loop, allowing for weak interactions between them. These weak interactions may become more important once the loss of A2058 interactions destabilizes drug binding, presumably resulting in a shift of the drug toward the other side of the tunnel, namely, to the vicinity of L22. Hence, the deletion of 15 residues from L22 may further destabilize telithromycin binding and confer telithromycin resistance. Such deletions may also lead to notable differences in the tunnel outline, as well as to an increase of its diameter to a size, allowing the progression of the nascent chain.
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; DNA, Bacterial/genetics ; Deinococcus/drug effects ; Deinococcus/genetics ; Drug Resistance, Bacterial ; Ketolides/chemistry ; Ketolides/pharmacology ; Microbial Sensitivity Tests ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Mycobacterium smegmatis/drug effects ; Mycobacterium smegmatis/genetics ; RNA, Bacterial/drug effects ; RNA, Bacterial/genetics ; RNA, Ribosomal, 23S/genetics ; Ribosomal Proteins/genetics ; Ribosomal Proteins/physiology ; Sequence Deletion ; Structure-Activity Relationship
Chemical Substances	Anti-Bacterial Agents ; DNA, Bacterial ; Ketolides ; RNA, Bacterial ; RNA, Ribosomal, 23S ; Ribosomal Proteins ; telithromycin (KI8H7H19WL)
Language	English
Publishing date	2006-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/AAC.00767-06
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Article: Desensitization to gonadotropic hormones: a model system for the regulation of a G-protein-coupled receptor with 7-transmembrane spanning regions.

Hirsh, Liron / Ben-Ami, Ido / Freimann, Sarit / Dantes, Ada / Tajima, Kimihisa / Kotsuji, Fumikazu / Amsterdam, Abraham

Biochemical and biophysical research communications

2005 Volume 326, Issue 1, Page(s) 1–6

Abstract: ... activation of G-coupled receptors, which activate the hormone sensitive adenylyl cyclase, protein kinase ... in other G-coupled-7-transmembrane receptor system is also discussed. ...

Abstract	Gonadotropic hormone, luteinizing hormone, and follicle-stimulating hormone exert their effect via activation of G-coupled receptors, which activate the hormone sensitive adenylyl cyclase, protein kinase A, and cyclic AMP responsive elements. This activation leads to specific de novo synthesis of steroidogenic factors and steroidogenic enzymes. In normal cells and following activation of this signaling pathway, desensitization period will be followed. This down-regulation, which was studied in detail for the last three decays, was found to take place at various steps of these signal transduction pathways as well as at different kinetics. A common and diverse feature of the mechanism of desensitization in other G-coupled-7-transmembrane receptor system is also discussed.
MeSH term(s)	Adenylyl Cyclases/metabolism ; Animals ; Cell Membrane/metabolism ; Down-Regulation/physiology ; Female ; Follicle Stimulating Hormone/metabolism ; Gene Expression Regulation/physiology ; Gonadotropins/metabolism ; Humans ; Luteinizing Hormone/metabolism ; Male ; Mitogen-Activated Protein Kinases/metabolism ; Models, Biological ; Phosphorylation ; Protein Structure, Tertiary ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction/physiology
Chemical Substances	Gonadotropins ; Receptors, G-Protein-Coupled ; Luteinizing Hormone (9002-67-9) ; Follicle Stimulating Hormone (9002-68-0) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Adenylyl Cyclases (EC 4.6.1.1)
Language	English
Publishing date	2005-01-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2004.10.168
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