susana alemany (0000-0002-4089-7620)

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Biography

Susana Alemany de la Peña (Madrid, 1956) is Senior Research at the Spanish Research Council (CSIC) and has been Biology and Biomedicine Area Coordinator of CSIC (2017-2019). She has been director of the Institute of Biomedical Research Alberto Sols, co-shared by CSIC and UAM (2013-2014) and is author of numerous original scientific articles published in international journals in the field of metabolism, infection tolerance mechanism, inflammation, intracellular signaling, infections and immunology. Actually she is head of group centered to investigate the role of inflammation in pathological processes and the cellular responses involved in this program. Understanding this system is critical, not only because of its importance in defense against infection and tissue damage, but also because the uncontrolled production of inflammatory mediators during sterile inflammatory pathologies is a major cause of many diseases, including rheumatoid arthritis, psoriasis, lupus, septic shock and malaria.

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Instituto de Investigaciones Biomedicas Alberto Sols: Madrid, Madrid, ES

1991-01-01 to present | Dr. (Metabolism and Cellular Signalling)

Employment

susana alemany

https://orcid.org/0000-0002-4089-7620

Personal information

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Biography

Activities

Employment (1)

Instituto de Investigaciones Biomedicas Alberto Sols: Madrid, Madrid, ES

Education and qualifications (3)

Fundacion Jimenez Diaz: Madrid, Madrid, ES

University of Dundee College of Life Sciences: Dundee, Dundee, GB

Fundacion Jimenez Diaz: Madrid, Madrid, ES

Funding (8)

Cot/tpl-2 en la señalización por IL-1

Identificación de mecanismos moleculares involucrados en la alteración de la hematopoiesis homeostática

Mecanismos de actuación de Cot

Papel de Cot/tpl2 en procesos inflamatorios mediados por macrófagos

Regulation of proto-oncogenic Cot Kinase activity

Role of Cot/tpl2 in the generation of the different Th lymphocytes and its influence in the development of allergic-asthma

Sobreexpresion de Cot/tpl2 en tumores

Tironet2

Works (50 of 60)

Abnormal Dendritic Cell-poiesis in Patients With Lower-risk Myelodysplastic Syndromes.

Hematopoiesis in aged female mice devoid of thyroid hormone receptors.

Thyroid Hormone Receptor β Inhibits Self-Renewal Capacity of Breast Cancer Stem Cells.

Common and Differential Transcriptional Actions of Nuclear Receptors Liver X Receptors α and β in Macrophages.

SIRT1 Controls Acetaminophen Hepatotoxicity by Modulating Inflammation and Oxidative Stress

Influence of Preparation Methods of Chitooligosaccharides on Their Physicochemical Properties and Their Anti-Inflammatory Effects in Mice and in RAW264.7 Macrophages.

Myeloid cell deficiency of p38γ/p38δ protects against candidiasis and regulates antifungal immunity.

Map3k8 controls granulocyte colony-stimulating factor production and neutrophil precursor proliferation in lipopolysaccharide-induced emergency granulopoiesis

Map3k8 Modulates Monocyte State and Atherogenesis in ApoE(-/-) Mice

The Thyroid Hormone Receptors Inhibit Hepatic Interleukin-6 Signaling During Endotoxemia

Metabolic signatures linked to macrophage polarization: From glucose metabolism to oxidative phosphorylation

The Tpl2 kinase regulates the COX-2/prostaglandin E2 axis in adipocytes in inflammatory conditions

Cot/tpl2 participates in the activation of macrophages by adiponectin

Sterile inflammation in acetaminophen-induced liver injury is mediated by Cot/tpl2

Corrigendum to " Involvement of Cot activity in the proliferation of ALCL lymphoma cells" [Biochem. Biophys. Res. Commun. 411 (2011) 655-660]

Cot/tpl2-MKK1/2-Erk1/2 controls mTORC1-mediated mRNA translation in Toll-like receptor-activated macrophages

Cot/tpl2 activity is required for TLR-induced activation of the Akt p70 S6k pathway in macrophages: Implications for NO synthase 2 expression

Involvement of Cot activity in the proliferation of ALCL lymphoma cells

Cot/tpl2 (MAP3K8) mediates myeloperoxidase activity and hypernociception following peripheral inflammation

COX2 expression and Erk1/Erk2 activity mediate Cot-induced cell migration

Bruton's tyrosine kinase is not essential for LPS-induced activation of human monocytes

TRAF6 and Src kinase activity regulates Cot activation by IL-1

15-Deoxy-Δ12,14-prostaglandin J2 Regulates Endogenous Cot MAPK Kinase Kinase 1 Activity Induced by Lipopolysaccharide

The COOH-terminal domain of wild-type Cot regulates its stability and kinase specific activity

Cot Kinase Induces Cyclooxygenase-2 Expression in T Cells through Activation of the Nuclear Factor of Activated T Cells

P27kif protein levels and E2F activity are targets of cot kinase during G1 phase progression in T cells

Regulation of cyclooxygenase activity by metamizol

Cot kinase activates tumor necrosis factor-α gene expression in a cyclosporin a-resistant manner

Cot Kinase Regulation of IL-2 Production in Jurkat T Cells

Regulation of ERK2 dephosphorylation in G1-stimulated rat T lymphoblasts

Interleukin-2 induces γ-S-adenosyl-L-methionine synthetase gene expression during T-lymphocyte activation

The Catalytic Domain of pp56lck, but Not Its Regulatory Domain, Is Sufficient for Inducing IL-2 Production

β-endorphin in immunosuppression and analgesia | β-ENDORFINA EN IMMUNOSUPRESION Y ANALGESIA

Induction of NGFI-B gene expression during T cell activation: Role of protein phosphatases

Raf-1 and ERK2 kinases are required for phorbol 12,13-dibutyrate-stimulated proliferation of rat lymphoblasts. ERK2 activation precedes Raf-1 hyperphosphorylation

NGFI-A gene expression is necessary for T lymphocyte proliferation

β-Endorphin inhibits interleukin-2 release and expression of interleukin- 2 receptors in concanavalin A-stimulated splenic lymphocytes

Modulation of casein kinase II activity by the polar head group of an insulin-sensitive glycosyl-phosphatidylinositol

Phospho-oligosaccharide dependent phosphorylation of ATP citrate lyase

Phosphorylation control by insulin in adipocytes is interfered with at a post-receptor step by phosphoinositol and glucosamine

Conversion of rat liver S-adenosyl-l-methionine synthetase from high-Mr form to low-Mr form by LiBr

Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle

Purification and comparison of two forms of S-adenosyl-L-methionine synthetase from rat liver

Specific loss of the high-molecular-weight form of S-adenosyl-L-methionine synthetase in human liver cirrhosis

Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of a type-2A protein phosphatase

Phospho-dephospho-control by insulin is mimicked by a phospho- oligosaccharide in adipocytes

Phosphorylase a is an allosteric inhibitor of the glycogen and microsomal forms of rat hepatic protein phosphatase-1

The protein phosphatases involved in cellular regulation. Evidence that dephosphorylation of glycogen phosphorylase and glycogen synthase in the glycogen and microsomal fractions of rat liver are catalysed by the same enzyme: Protein phosphatase-1

The protein phosphatases involved in cellular regulation. 2. Purification, subunit structure and properties of protein phosphatases-2A0, 2A1, and 2A2 from rabbit skeletal muscle

Purification and photoaffinity labelling of lipid methyltransferase from rat liver