Her primary scientific interests are in Cell biology, Biochemistry, Nuclear export signal, Molecular biology and Nucleoporin. Her Cell biology study frequently links to adjacent areas such as snRNP. Her study connects Biophysics and Biochemistry.
Her work carried out in the field of Nuclear export signal brings together such families of science as Ran, Xenopus and RNA-binding protein. Her Molecular biology study combines topics from a wide range of disciplines, such as RNA splicing, Spliceosome and Mutant. The Nucleoporin study which covers Cytoplasm that intersects with Nuclear protein and Inflammation.
Angela Bachi mainly investigates Cell biology, Biochemistry, Proteomics, Molecular biology and Proteome. Angela Bachi has researched Cell biology in several fields, including Cell growth, DNA damage and Cytoskeleton. Her research on Biochemistry frequently links to adjacent areas such as Biophysics.
Her Proteomics study integrates concerns from other disciplines, such as Cysteine and Computational biology. Her Molecular biology research incorporates themes from RNA, RNA splicing, Nuclear protein and Mutant. The various areas that Angela Bachi examines in her Proteome study include Peptide library, Chromatography and Ligand.
Cell biology, Cancer research, Proteomics, Computational biology and DNA damage are her primary areas of study. Her Cell biology research is multidisciplinary, incorporating elements of Messenger RNA and Cell growth. Her biological study spans a wide range of topics, including Carcinogenesis, Cancer, Tumor Status, Tumor microenvironment and Proteasome.
Her study in Proteomics is interdisciplinary in nature, drawing from both Proteome and Brain tumor. Her DNA damage research is multidisciplinary, incorporating perspectives in Embryonic stem cell, Embryo, Embryogenesis, Endogeny and Transcription. Endonuclease is a primary field of her research addressed under Biochemistry.
Her primary areas of investigation include Cell biology, DNA replication, Molecular biology, Stable isotope labeling by amino acids in cell culture and Proteomics. Her research links Decapping complex with Cell biology. Her work deals with themes such as Cell division and DNA-binding protein, which intersect with DNA replication.
Her studies deal with areas such as RNA, RNA splicing, snRNP, Transcriptional regulation and Intron as well as Molecular biology. The Stable isotope labeling by amino acids in cell culture study combines topics in areas such as Extracellular, Receptor and Contraction. Angela Bachi interconnects Sample, Sample preparation and Tandem mass spectrometry in the investigation of issues within Proteomics.
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Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion
Tiziana Bonaldi;Fabio Talamo;Paola Scaffidi;Denise Ferrera.
The EMBO Journal (2003)
TAP, the Human Homolog of Mex67p, Mediates CTE-Dependent RNA Export from the Nucleus
Patric Grüter;Carlos Tabernero;Cayetano von Kobbe;Christel Schmitt.
Molecular Cell (1998)
Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes.
Maddalena Fratelli;Hans Demol;Magda Puype;Simona Casagrande.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release
Emilie Venereau;Maura Casalgrandi;Milena Schiraldi;Daniel J. Antoine.
Journal of Experimental Medicine (2012)
HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4
Milena Schiraldi;Angela Raucci;Laura Martínez Muñoz;Elsa Livoti.
Journal of Experimental Medicine (2012)
REF, an evolutionary conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export.
Françoise Stutz;Angela Bachi;Tobias Doerks;Isabelle C. Braun.
PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation.
Mutsuhito Ohno;Alexandra Segref;Angela Bachi;Matthias Wilm.
A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro.
Tilmann Achsel;Hero Brahms;Berthold Kastner;Angela Bachi.
The EMBO Journal (1999)
A Common Core RNP Structure Shared between the Small Nucleoar Box C/D RNPs and the Spliceosomal U4 snRNP
Nicholas J Watkins;Véronique Ségault;Bruno Charpentier;Bruno Charpentier;Stephanie Nottrott.
The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates.
A. Bachi;I. C. Braun;J. P. Rodrigues;N. Panté.
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