Tamar Hanoch

发表

The nuclear translocation of the kinases p38 and JNK promotes inflammation-induced cancer

J. Blenis, R. Seger, G. Maik-Rachline, 2018, Science Signaling.

Mitotic HOOK3 phosphorylation by ERK1c drives microtubule-dependent Golgi destabilization and fragmentation

R. Seger, S. S. Yadav, I. Wortzel, 2021, iScience.

Mitotic Golgi translocation of ERK1c is mediated by a PI4KIIIβ–14-3-3γ shuttling complex

Z. Porat, R. Seger, I. Wortzel, 2015, Journal of Cell Science.

ERK1b, a 46‐kDa ERK isoform that is differentially regulated by MEK

Z. Yao, R. Seger, Y. Yung, 2022, Cell biology international.

Mechanisms of gonadotropin desensitization

R. Seger, J. Strauss, A. Amsterdam, 2002, Molecular and Cellular Endocrinology.

Differential Activation of Mitogen-activated Protein Kinase and S6 Kinase Signaling Pathways by 12-O-Tetradecanoylphorbol-13-acetate (TPA) and Insulin

A. Gazit, R. Seger, Y. Zick, 1995, The Journal of Biological Chemistry.

Conjugates of gonadotropin releasing hormone (GnRH) with carminic acid: Synthesis, generation of reactive oxygen species (ROS) and biological evaluation.

B. Mester, R. Seger, G. Gescheidt, 2008, Bioorganic & medicinal chemistry.

Hippocampal plasticity involves extensive gene induction and multiple cellular mechanisms

M. Bundman, E. Nedivi, M. Kornuc, 1998, Journal of Molecular Neuroscience.

Regulation of cell proliferation by ERK and signal-dependent nuclear translocation of ERK is dependent on Tm5NM1-containing actin filaments

Vanessa B. Sequeira, J. Stehn, E. Hardeman, 2015, Molecular biology of the cell.

Identification of a Cytoplasmic-Retention Sequence in ERK2*

H. Rubinfeld, R. Seger, Tamar Hanoch, 1999, The Journal of Biological Chemistry.

Inhibition of gonadotropin-stimulated steroidogenesis by the erk cascade

Revital Rosenberg, R. Seger, J. Strauss, 2019 .

The ERK Signaling Cascade Inhibits Gonadotropin-Stimulated Steroidogenesis

Revital Rosenberg, R. Seger, J. Strauss, 2001, The Journal of Biological Chemistry.

M. Ebert, C. Hopf, P. Kienle, 2016, Oncotarget.

Intrinsically active MEK variants are differentially regulated by proteinases and phosphatases

J. Fernández-Recio, F. Glaser, F. Gervasio, 2018, Scientific Reports.

Activation of Signaling Cascades by Weak Extremely Low Frequency Electromagnetic Fields

N. Kuster, M. Murbach, P. Bounds, 2017, Cellular Physiology and Biochemistry.

Gonadotropin-Releasing Hormone Induces Apoptosis of Prostate Cancer Cells

R. Seger, Z. Naor, S. Kraus, 2004, Cancer Research.

ECTO- AND EXO-PROTEIN KINASES IN SCHISTOSOMA MANSONI: REGULATION OF SURFACE PHOSPHORYLATION BY ACETYLCHOLINE AND IDENTIFICATION OF THE ALPHA SUBUNIT OF CKII AS A MAJOR SECRETED PROTEIN KINASE

R. Seger, S. Jeon, R. Arnon, 2005, The Journal of parasitology.

The nuclear translocation of ERK1/2 as an anticancer target

R. Seger, D. A. Berti, A. Plotnikov, 2015, Nature Communications.

The ERK signaling cascade inhibits gonadotropin-stimulated steroidogenesis.

Revital Rosenberg, R. Seger, J. Strauss, 2017, The Journal of Biological Chemistry.

Interaction with MEK Causes Nuclear Export and Downregulation of Peroxisome Proliferator-Activated Receptor γ

R. Seger, D. Chuderland, M. Meyer, 2006, Molecular and Cellular Biology.

Detection of partially phosphorylated forms of ERK by monoclonal antibodies reveals spatial regulation of ERK activity by phosphatases

R. Seger, D. Zharhary, R Seger, 2000, FEBS letters.

ERK1b, a 46-kDa ERK Isoform That Is Differentially Regulated by MEK*

R. Seger, Y. Yung, Tamar Hanoch, 2000, The Journal of Biological Chemistry.

Extracellular Signal-Regulated Kinase 1c (ERK1c), a Novel 42-Kilodalton ERK, Demonstrates Unique Modes of Regulation, Localization, and Function

R. Seger, Y. Shaul, D. Aebersold, 2004, Molecular and Cellular Biology.

Altered Regulation of ERK1b by MEK1 and PTP-SL and Modified Elk1 Phosphorylation by ERK1b Are Caused by Abrogation of the Regulatory C-terminal Sequence of ERKs*

R. Seger, D. Aebersold, Y. Yung, 2001, The Journal of Biological Chemistry.

Involvement of the Activation Loop of ERK in the Detachment from Cytosolic Anchoring*

H. Rubinfeld, R. Seger, Seunghee Yoon, 2001, The Journal of Biological Chemistry.

Detection of ERK activation by a novel monoclonal antibody

H. Rubinfeld, R. Seger, D. Zharhary, 1997, FEBS letters.

Nuclear translocation of mitogen-activated protein kinase kinase (MEK1) in response to mitogenic stimulation.

H. Rubinfeld, R. Seger, Tamar Hanoch, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The ERK Signaling Cascade Inhibits Gonadotropin-Stimulated Steroidogenesis

Revital Rosenberg, R. Seger, J. Strauss, 2023, Journal of biotechnology and biomedicine.

Stimulation of Jun N-terminal kinase (JNK) by gonadotropin-releasing hormone in pituitary alpha T3-1 cell line is mediated by protein kinase C, c-Src, and CDC42.

R. Seger, O. Benard, Z. Naor, 1998, Molecular endocrinology.