Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Monica J. S. Nadler"'
Autor:
Monica J. S. Nadler, Weipang Chang, Ekim Ozkaynak, Yuda Huo, Yi Nong, Morgane Boillot, Mark Johnson, Antonio Moreno, Matthew P. Anderson
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-17 (2023)
Human-specific SINE-VNTR-Alu (SVA) retrotransposons in neurodevelopmental genes CDK5RAP2 and SCN8A repress their expression to delay neuronal maturation. SVA-lncRNA AK057321 binds these SVAs to release gene repression and drive neuronal maturation.
Externí odkaz:
https://doaj.org/article/aca25956f52c469ba5776582c1a9a221
Publikováno v:
Ann Neurol
Objective Autism spectrum disorder (ASD) affects 1 in 59 children, yet except for rare genetic causes, the etiology in most ASD remains unknown. In the ASD brain, inflammatory cytokine and transcript profiling shows increased expression of genes enco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efb72d96b95ff6eef6d97d97f77a0d67
https://pubmed.ncbi.nlm.nih.gov/31591744
https://pubmed.ncbi.nlm.nih.gov/31591744
Autor:
Bodvael Pennarun, Anja Schempf, Bo Yang, Parisa Mousavi Shafaei, Da Yang, Dipak Datta, Barbara L. Hopkins, Steffi Oesterreich, Octavian Bucur, Thierry Bertomeu, John J. Skoko, Andrea Pelosi, Kenneth Ndebele, Carola A. Neumann, Kevin M. Levine, Monica J. S. Nadler, Maria Giulia Rizzo, Roya Khosravi-Far
Publikováno v:
Antioxidants & Redox Signaling
Precision in redox signaling is attained through posttranslational protein modifications such as oxidation of protein thiols. The peroxidase peroxiredoxin 1 (PRDX1) regulates signal transduction through changes in thiol oxidation of its cysteines. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d80e85936d2ed72d4b56a8d948e468c6
https://pubmed.ncbi.nlm.nih.gov/28398822
https://pubmed.ncbi.nlm.nih.gov/28398822
Autor:
Mark Duquette, Jack Lawler, Monica J. S. Nadler, Trevor J. Shuttleworth, Dayne Okuhara, Jill L. Thompson
Publikováno v:
Matrix biology : journal of the International Society for Matrix Biology
The thrombospondins (TSPs) are a family of matricellular proteins that regulate cellular phenotype through interactions with a myriad of other proteins and proteoglycans. We have identified a novel interaction of the members of the TSP gene family wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae0ff58c5a95cab85ca04d817477f57f
Poor antibody validation is a challenge in biomedical research: a case study for detection of c-FLIP
Autor:
Maria Sinziana Muraru, Thierry Bertomeu, Octavian Bucur, Andreea Lucia Stancu, Monica J. S. Nadler, Bodvael Pennarun, Roya Khosravi-Far
Publikováno v:
Apoptosis. 18:1154-1162
Successful translation of findings derived from preclinical studies into effective therapies is critical in biomedical research. Lack of robustness and reproducibility of the preclinical data, due to insufficient number of repeats, inadequate cell-ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa0b4a950ed45cd05648fa584937ce37
https://doi.org/10.1007/s10495-013-0880-0
https://doi.org/10.1007/s10495-013-0880-0
Autor:
Kathryn G. Klemic, Abdallah Badou, Usha Govindarajulu, Judith Stein, Jean-Pierre Kinet, Didi Matza, Oz M. Shapira, Leonard K. Kaczmarek, Richard A. Flavell, Amnon Peled, Monica J. S. Nadler
Publikováno v:
PLoS ONE, Vol 11, Iss 1, p e0147379 (2016)
PLoS ONE
PLoS ONE
The process of calcium entry in T cells is a multichannel and multi-step process. We have studied the requirement for L-type calcium channels (Cav1.1) α1S subunits during calcium entry after TCR stimulation. High expression levels of Cav1.1 channels
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f473a86f9e6ab7c2ca562fc38c3842ff
http://europepmc.org/articles/PMC4729531?pdf=render
http://europepmc.org/articles/PMC4729531?pdf=render
Autor:
Meredith C. Hermosura, Qiqin Zhu, Alexander J. Stokes, Anne-Laure Perraud, Andrew M. Scharenberg, Reinhold Penner, Kazunori Inabe, Tomohiro Kurosaki, Andrea Fleig, Jean-Pierre Kinet, Monica J. S. Nadler
Publikováno v:
Nature. 411:590-595
The molecular mechanisms that regulate basal or background entry of divalent cations into mammalian cells are poorly understood. Here we describe the cloning and functional characterization of a Ca2+- and Mg2+-permeable divalent cation channel, LTRPC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f522579c27004ec98e6519faee4f621
https://doi.org/10.1038/35079092
https://doi.org/10.1038/35079092
Autor:
Nobumichi Hozumi, Jenny Jongstra-Bilen, Joan E. Wither, Noemi Fusaki, Yongjian Wu, Laurie A. Brennan, John F. Timms, Nobuhiko Tada, Monica J. S. Nadler, Gerald D. Gish, Tony Pawson, Benjamin G. Neel
Publikováno v:
Current Biology. 8(18):1009-1017
Background: Signals from the B-cell antigen receptor (BCR) help to determine B-cell fate, directing either proliferation, differentiation, or growth arrest/apoptosis. The protein tyrosine phosphatase SHP-1 is known to regulate the strength of BCR sig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99a1d62f0638777b91e61815638618e6
Autor:
Haiyan Chen, Haihua Gu, Monica J. S. Nadler, Larry R. Rohrschneider, Benjamin G. Neel, Shubhangi Kamatkar, Kristen Carlberg, John F. Timms
Publikováno v:
Molecular and Cellular Biology. 18:3838-3850
The protein tyrosine phosphatase SHP-1 is a critical regulator of macrophage biology, but its detailed mechanism of action remains largely undefined. SHP-1 associates with a 130-kDa tyrosyl-phosphorylated species (P130) in macrophages, suggesting tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32cde7c637b0f088327527a6761afc5e
https://doi.org/10.1128/mcb.18.7.3838
https://doi.org/10.1128/mcb.18.7.3838
Publikováno v:
Journal of Biological Chemistry. 272:20038-20043
The inhibitory Fc receptor, FcgammaRIIB, provides a signal that aborts B cell antigen receptor activation, blocking extracellular calcium influx. Because the protein-tyrosine phosphatase SHP-1 binds tyrosyl phosphorylated FcgammaRIIB and FcgammaRIIB-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09ac4823f2431d1a88e0de5923d23e7b
https://doi.org/10.1074/jbc.272.32.20038
https://doi.org/10.1074/jbc.272.32.20038