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Article ; Online: G-quadruplexes rescuing protein folding.

Son, Ahyun / Huizar Cabral, Veronica / Huang, Zijue / Litberg, Theodore J / Horowitz, Scott

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

2023 Volume 120, Issue 20, Page(s) e2216308120

Abstract: Maintaining the health of the proteome is a critical cellular task. Recently, we found G-quadruplex ...

Abstract	Maintaining the health of the proteome is a critical cellular task. Recently, we found G-quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in vitro and could at least indirectly improve the protein folding environment of
MeSH term(s)	G-Quadruplexes ; Escherichia coli/genetics ; Protein Aggregates ; Nucleic Acids ; Protein Folding
Chemical Substances	Protein Aggregates ; Nucleic Acids
Language	English
Publishing date	2023-05-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2216308120
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Article ; Online: Autoantibodies targeting G protein-coupled receptors: An evolving history in autoimmunity. Report of the 4th international symposium.

Cabral-Marques, Otávio / Moll, Guido / Catar, Rusan / Preuß, Beate / Bankamp, Lukas / Pecher, Ann-Christin / Henes, Joerg / Klein, Reinhild / Kamalanathan, A S / Akbarzadeh, Reza / van Oostveen, Wieke / Hohberger, Bettina / Endres, Matthias / Koolmoes, Bryan / Levarht, Nivine / Postma, Rudmer / van Duinen, Vincent / van Zonneveld, Anton Jan / de Vries-Bouwstra, Jeska /

Fehres, Cynthia / Tran, Florian / do Vale, Fernando Yuri Nery / da Silva Souza, Kamilla Batista / Filgueiras, Igor Salerno / Schimke, Lena F / Baiocchi, Gabriela Crispim / de Miranda, Gustavo Cabral / da Fonseca, Dennyson Leandro Mathias / Freire, Paula Paccielli / Hackel, Alexander M / Grasshoff, Hanna / Stähle, Anja / Müller, Antje / Dechend, Ralf / Yu, Xinhua / Petersen, Frank / Sotzny, Franziska / Sakmar, Thomas P / Ochs, Hans D / Schulze-Forster, Kai / Heidecke, Harald / Scheibenbogen, Carmen / Shoenfeld, Yehuda / Riemekasten, Gabriela

Autoimmunity reviews

2023 Volume 22, Issue 5, Page(s) 103310

Abstract: G protein-coupled receptors (GPCR) are involved in various physiological and ... e.g., systemic sclerosis and systemic lupus erythematosus). Beyond their association with disease ...

Abstract	G protein-coupled receptors (GPCR) are involved in various physiological and pathophysiological processes. Functional autoantibodies targeting GPCRs have been associated with multiple disease manifestations in this context. Here we summarize and discuss the relevant findings and concepts presented in the biennial International Meeting on autoantibodies targeting GPCRs (the 4th Symposium), held in Lübeck, Germany, 15-16 September 2022. The symposium focused on the current knowledge of these autoantibodies' role in various diseases, such as cardiovascular, renal, infectious (COVID-19), and autoimmune diseases (e.g., systemic sclerosis and systemic lupus erythematosus). Beyond their association with disease phenotypes, intense research related to the mechanistic action of these autoantibodies on immune regulation and pathogenesis has been developed, underscoring the role of autoantibodies targeting GPCRs on disease outcomes and etiopathogenesis. The observation repeatedly highlighted that autoantibodies targeting GPCRs could also be present in healthy individuals, suggesting that anti-GPCR autoantibodies play a physiologic role in modeling the course of diseases. Since numerous therapies targeting GPCRs have been developed, including small molecules and monoclonal antibodies designed for treating cancer, infections, metabolic disorders, or inflammatory conditions, anti-GPCR autoantibodies themselves can serve as therapeutic targets to reduce patients' morbidity and mortality, representing a new area for the development of novel therapeutic interventions.
MeSH term(s)	Humans ; Autoantibodies ; Autoimmunity ; COVID-19 ; Autoimmune Diseases ; Receptors, G-Protein-Coupled/metabolism
Chemical Substances	Autoantibodies ; Receptors, G-Protein-Coupled
Language	English
Publishing date	2023-03-10
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2144145-5
ISSN	1873-0183 ; 1568-9972
ISSN (online)	1873-0183
ISSN	1568-9972
DOI	10.1016/j.autrev.2023.103310
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Zs.A 5913: Show issues

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Article ; Online: Pre-miRNA-149 G-quadruplex as a molecular agent to capture nucleolin.

Santos, Tiago / Miranda, André / Imbert, Lionel / Jardim, Andreia / Caneira, Catarina R F / Chu, Virgínia / Conde, João P / Campello, Maria Paula Cabral / Paulo, António / Salgado, Gilmar / Cabrita, Eurico J / Cruz, Carla

European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences

2021 Volume 169, Page(s) 106093

Abstract: ... of an appropriate biomolecular receptor. Recently, RNA G-quadruplexes emerged as plausible receptors due ... the capability of the precursor microRNA 149 to form a G-quadruplex structure and determined the role ... that some ligands may have in its folding and binding capacity to nucleolin. The G-quadruplex formation was induced ...

Abstract	One of the most significant challenges in capturing and detecting biomarkers is the choice of an appropriate biomolecular receptor. Recently, RNA G-quadruplexes emerged as plausible receptors due to their ability to recognize with high-affinity proteins. Herein, we have unveiled and characterized the capability of the precursor microRNA 149 to form a G-quadruplex structure and determined the role that some ligands may have in its folding and binding capacity to nucleolin. The G-quadruplex formation was induced by K
MeSH term(s)	Cell Line ; G-Quadruplexes ; Humans ; MicroRNAs/genetics ; Molecular Docking Simulation ; Phosphoproteins/genetics ; RNA-Binding Proteins/genetics ; Nucleolin
Chemical Substances	MIRN149 microRNA, human ; MicroRNAs ; Phosphoproteins ; RNA-Binding Proteins
Language	English
Publishing date	2021-12-16
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1154366-8
ISSN	1879-0720 ; 0928-0987
ISSN (online)	1879-0720
ISSN	0928-0987
DOI	10.1016/j.ejps.2021.106093
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Zs.A 3705: Show issues

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Article ; Online: G-Protein Phosphorylation

Celio Cabral Oliveira / Alan M. Jones / Elizabeth Pacheco Batista Fontes / Pedro A. Braga dos Reis

International Journal of Molecular Sciences, Vol 23, Iss 6544, p

Aspects of Binding Specificity and Function in the Plant Kingdom

2022 Volume 6544

Abstract: ... composition in plants. The transduction of signals occurs in part by a simple repertoire of heterotrimeric G ... proteins, with a core composed of α-, β-, and γ-subunits, together with a 7-transmembrane Regulator G ... Signaling (RGS) protein. With a small repertoire of G proteins in plants, phosphorylation by receptor ...

Abstract	Plant survival depends on adaptive mechanisms that constantly rely on signal recognition and transduction. The predominant class of signal discriminators is receptor kinases, with a vast member composition in plants. The transduction of signals occurs in part by a simple repertoire of heterotrimeric G proteins, with a core composed of α-, β-, and γ-subunits, together with a 7-transmembrane Regulator G Signaling (RGS) protein. With a small repertoire of G proteins in plants, phosphorylation by receptor kinases is critical in regulating the active state of the G-protein complex. This review describes the in vivo detected phosphosites in plant G proteins and conservation scores, and their in vitro corresponding kinases. Furthermore, recently described outcomes, including novel arrestin-like internalization of RGS and a non-canonical phosphorylation switching mechanism that drives G-protein plasticity, are discussed.
Keywords	phosphorylation ; G protein ; RGS ; GPA1 ; AGB1 ; XLG ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	580
Language	English
Publishing date	2022-06-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Differential regulation of G protein signaling in

Watkins, Justin M / Ross-Elliott, Timothy J / Shan, Xiaoyi / Lou, Fei / Dreyer, Bernd / Tunc-Ozdemir, Meral / Jia, Haiyan / Yang, Jing / Oliveira, Celio Cabral / Wu, Luguang / Trusov, Yuri / Schwochert, Timothy D / Krysan, Patrick / Jones, Alan M

Science signaling

2021 Volume 14, Issue 695

Abstract: ... arrest cytoplasmic G protein-mediated signaling, depending on the bias of the receptor or ligand ...

Abstract	In animals, endocytosis of a seven-transmembrane GPCR is mediated by arrestins to propagate or arrest cytoplasmic G protein-mediated signaling, depending on the bias of the receptor or ligand, which determines how much one transduction pathway is used compared to another. In
MeSH term(s)	Animals ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Arrestins ; Endocytosis ; GTP-Binding Proteins ; RGS Proteins ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction ; beta-Arrestins
Chemical Substances	Arabidopsis Proteins ; Arrestins ; RGS Proteins ; RGS1 protein, Arabidopsis ; Receptors, G-Protein-Coupled ; beta-Arrestins ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2021-08-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.abe4090
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Article ; Online: Targeting proto-oncogene B-MYB G-quadruplex with a nucleic acid-based fluorescent probe.

Lourenço, Pedro / Miranda, André / Campello, Maria Paula Cabral / Paulo, António / Louis-Mergny, Jean / Cruz, Carla

International journal of biological macromolecules

2024 Volume 266, Issue Pt 1, Page(s) 131055

Abstract: ... therapy. Oncogenes often contain DNA structures called G-quadruplexes (G4s) in their promoter regions, and ...

Abstract	The B-MYB gene encodes a transcription factor (B-MYB) that regulates cell growth and survival. Abnormal expression of B-MYB is frequently observed in lung cancer and poses challenges for targeted drug therapy. Oncogenes often contain DNA structures called G-quadruplexes (G4s) in their promoter regions, and B-MYB is no exception. These G4s play roles in genetic regulation and are potential cancer treatment targets. In this study, a probe was designed to specifically identify a G4 within the promoter region of the B-MYB gene. This probe combines an acridine derivative ligand with a DNA segment complementary to the target sequence, enabling it to hybridize with the adjacent sequence of the G4 being investigated. Biophysical studies demonstrated that the acridine derivative ligands C
MeSH term(s)	G-Quadruplexes ; Humans ; Fluorescent Dyes/chemistry ; Promoter Regions, Genetic ; Proto-Oncogene Mas ; Ligands ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Trans-Activators/chemistry ; Acridines/chemistry ; Acridines/pharmacology ; Cell Cycle Proteins
Chemical Substances	Fluorescent Dyes ; Proto-Oncogene Mas ; MYBL2 protein, human ; Ligands ; MAS1 protein, human ; Trans-Activators ; Acridines ; Cell Cycle Proteins
Language	English
Publishing date	2024-03-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2024.131055
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Book ; Online: G-RAID

de Vos-de Jong, C.J. / Taylor, R.A. / Simons, R.R.I. / Roberts, H. / Hultén, C. / de Koeijer, A.A. / Lyytikäinen, T. / Napp, S. / Boklund, A. / Petie, R. / Sörén, K. / Swanenburg, M. / Comin, A. / Seppä-Lassila, L. / Cabral, M. / Snary, E.

Assessing the incursion risk of African swine fever virus using generic risk assessment tools

2019

Keywords	Life Science
Language	English
Publisher	Wageningen University & Research
Publishing country	nl
Document type	Book ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Book ; Online: G-RAID

Snary, E.L. / Taylor, R.A. / Simons, R.R.L. / Roberts, H. / Hultén, C. / de Koeijer, A.A. / Lyytikäinen, T. / Napp, S. / Boklund, A. / Petie, R. / Sörén, K. / Swanenburg, M. / Comin, A. / Seppä-Lässila, L. / Labato Guimarães Ferraira Cabral, Maria / de Vos-de Jong, C.J.

Generic risk assessment tools for infectious animal disease incursion

2019

Keywords	Life Science
Language	English
Publishing country	nl
Document type	Book ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: G-Protein Phosphorylation: Aspects of Binding Specificity and Function in the Plant Kingdom.

Oliveira, Celio Cabral / Jones, Alan M / Fontes, Elizabeth Pacheco Batista / Reis, Pedro A Braga Dos

International journal of molecular sciences

2022 Volume 23, Issue 12

Abstract	Plant survival depends on adaptive mechanisms that constantly rely on signal recognition and transduction. The predominant class of signal discriminators is receptor kinases, with a vast member composition in plants. The transduction of signals occurs in part by a simple repertoire of heterotrimeric G proteins, with a core composed of α-, β-, and γ-subunits, together with a 7-transmembrane Regulator G Signaling (RGS) protein. With a small repertoire of G proteins in plants, phosphorylation by receptor kinases is critical in regulating the active state of the G-protein complex. This review describes the in vivo detected phosphosites in plant G proteins and conservation scores, and their in vitro corresponding kinases. Furthermore, recently described outcomes, including novel arrestin-like internalization of RGS and a non-canonical phosphorylation switching mechanism that drives G-protein plasticity, are discussed.
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; GTP-Binding Protein alpha Subunits/metabolism ; Heterotrimeric GTP-Binding Proteins/metabolism ; Phosphorylation ; Phosphotransferases/metabolism ; Plant Proteins/metabolism ; Plants/metabolism ; RGS Proteins/genetics ; RGS Proteins/metabolism
Chemical Substances	Arabidopsis Proteins ; GTP-Binding Protein alpha Subunits ; Plant Proteins ; RGS Proteins ; Phosphotransferases (EC 2.7.-) ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1)
Language	English
Publishing date	2022-06-11
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23126544
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Article ; Online: X-linked hypophosphatemia in 4 generations due to an exon 13-15 duplication in PHEX, in the absence of the c.*231A>G variant.

Soto Barros, Julio / Sanchez, Sabrina I / Cabral, Kristin / Beggs, Alan H / Agrawal, Pankaj B / Genetti, Casie A / Brownstein, Catherine A / Carpenter, Thomas O

Bone

2023 Volume 172, Page(s) 116763

Abstract: ... base change in the 3' untranslated region (UTR) (c.*231A>G) is reported as prevalent in North America ... Recently an exon 13-15 duplication has been found to occur in concert with the c.*231A>G variant, and ...

Abstract	X-linked hypophosphatemia is the most common cause of inherited rickets, due to inactivating variants of PHEX. More than 800 variants have been described to date and one which consists of a single base change in the 3' untranslated region (UTR) (c.231A>G) is reported as prevalent in North America. Recently an exon 13-15 duplication has been found to occur in concert with the c.231A>G variant, and thus it is unclear whether the pathogenicity is solely a function of the UTR variant. We present a family with XLH who harbors the exon 13-15 duplication but does not carry the 3'UTR variant, providing evidence that the duplication itself is the pathogenic variant when these two variants are found in cis.
MeSH term(s)	Humans ; Familial Hypophosphatemic Rickets/genetics ; Familial Hypophosphatemic Rickets/pathology ; PHEX Phosphate Regulating Neutral Endopeptidase/genetics ; Exons/genetics ; Genetic Diseases, X-Linked ; 3' Untranslated Regions ; Hypophosphatemia/genetics ; Mutation
Chemical Substances	PHEX Phosphate Regulating Neutral Endopeptidase (EC 3.4.24.-) ; 3' Untranslated Regions ; PHEX protein, human (EC 3.4.24.-)
Language	English
Publishing date	2023-04-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	632515-4
ISSN	1873-2763 ; 8756-3282
ISSN (online)	1873-2763
ISSN	8756-3282
DOI	10.1016/j.bone.2023.116763
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Zs.A 1571: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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