Results 21 to 30 of about 27,519 (289)

The scaffolding function of LSD1 controls DNA methylation in mouse ESCs

open access: yesNature Communications
Lysine-specific histone demethylase 1 (LSD1), which demethylates mono- or di- methylated histone H3 on lysine 4 (H3K4me1/2), is essential for early embryogenesis and development.
Sandhya Malla   +24 more
doaj   +2 more sources

Novel dual LSD1/HDAC6 inhibitor for the treatment of cancer

open access: goldPLoS ONE, 2023
Dually targeting the epigenetic proteins lysine specific demethylase 1 (LSD1) and histone deacetylases (HDACs) that play a key role in cancer cells by modulating gene repressor complexes including CoREST will have a profound effect in inhibiting tumour ...
Chandru Gajendran   +10 more
openalex   +3 more sources

412 Synergistic Targeting of Lysine-specific demethylase 1 (LSD1) and MAPK Signaling: A Mechanism-Guided Therapeutic Approach for Glioblastoma (GBM) [PDF]

open access: goldJournal of Clinical and Translational Science
OBJECTIVES/GOALS: LSD1 is a histone demethylase important in GBM regulation. Our goal is to design a therapeutic strategy for LSD1 inhibitors to meet clinical needs in GBM. Despite the abundance of LSD1 inhibitors, resistance emerges in GBM mouse models.
Lea Stitzlein   +8 more
doaj   +2 more sources

ZebraShare: a new venue for rapid dissemination of zebrafish mutant data [PDF]

open access: yesPeerJ, 2021
Background In the past decade, the zebrafish community has widely embraced targeted mutagenesis technologies, resulting in an abundance of mutant lines.
April DeLaurier   +13 more
doaj   +2 more sources

OTUD7B Deubiquitinates LSD1 to Govern Its Binding Partner Specificity, Homeostasis, and Breast Cancer Metastasis

open access: yesAdvanced Science, 2021
Genomic amplification of OTUD7B is frequently found across human cancers. But its role in tumorigenesis is poorly understood. Lysine‐specific demethylase 1 (LSD1) is known to execute epigenetic regulation by forming corepressor complex with CoREST ...
Zhicheng Gong   +13 more
doaj   +1 more source

Comparison of pharmacological inhibitors of lysine-specific demethylase 1 in glioblastoma stem cells reveals inhibitor-specific efficacy profiles

open access: yesFrontiers in Neurology, 2023
IntroductionImproved therapies for glioblastoma (GBM) are desperately needed and require preclinical evaluation in models that capture tumor heterogeneity and intrinsic resistance seen in patients.
Lea M. Stitzlein   +17 more
doaj   +1 more source

LSD1: Biologic Roles and Therapeutic Targeting [PDF]

open access: yesEpigenomics, 2016
LSD1 (KDM1A; BHC110; AOF2) was the first protein reported to exhibit histone demethylase activity and has since been shown to have multiple essential roles in mammalian biology. Given its enzymatic activity and its high-level expression in many human malignancies, a significant recent focus has been the development of pharmacologic inhibitors.
Maiques-Diaz, Alba, Somervaille, Tim Cp
openaire   +3 more sources

Genome-Wide Studies of Histone Demethylation Catalysed by the Fission Yeast Homologues of Mammalian LSD1 [PDF]

open access: yes, 2007
In order to gain a more global view of the activity of histone demethylases, we report here genome-wide studies of the fission yeast SWIRM and polyamine oxidase (PAO) domain homologues of mammalian LSD1. Consistent with previous work we find that the two
Abdelhalim Boukaba   +48 more
core   +12 more sources

Integrative analysis reveals histone demethylase LSD1 promotes RNA polymerase II pausing

open access: yesiScience, 2022
Summary: Lysine-specific demethylase 1 (LSD1) is well-known for its role in decommissioning enhancers during mouse embryonic stem cell (ESC) differentiation.
Hani Jieun Kim   +5 more
doaj   +1 more source

LSD1 inhibitors for cancer treatment: Focus on multi-target agents and compounds in clinical trials

open access: yesFrontiers in Pharmacology, 2023
Histone lysine-specific demethylase 1 (LSD1/KDM1A) was first identified in 2004 as an epigenetic enzyme able to demethylate specific lysine residues of histone H3, namely H3K4me1/2 and H3K9me1/2, using FAD as the cofactor.
Beatrice Noce   +3 more
semanticscholar   +1 more source

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