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LBH589
Known as:
(2E)-N-hydroxy-3-(4-(((2-(2-methyl-1h-indol-3-yl)ethyl)amino)methyl)phenyl)prop-2-enamide
, LBH 589
, NVP-LBH589
Â
Â
National Institutes of Health
Topic mentions per year
Topic mentions per year
2004-2018
0
10
20
30
2004
2018
Related topics
Related topics
1 relation
Broader (1)
panobinostat
Related mentions per year
Related mentions per year
2000-2018
2000
2005
2010
2015
2020
LBH589
panobinostat
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2011
2011
HDAC Inhibition by LBH589 Affects Phenotype and Function of Human Myeloid Dendritic Cells
W. Song
,
Y. I. Tai
,
+6 authors
N. C. Munshi
Leukemia
2011
LBH589 is a novel pan-histone deacetylase (HDAC) inhibitor that has potent antitumor activity in multiple myeloma and other…Â
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2009
2009
DNA microarray profiling of genes differentially regulated by the histone deacetylase inhibitors vorinostat and LBH589 in colon cancer cell lines
Melissa Janae Labonte
,
Peter Murray Wilson
,
William Fazzone
,
Susan Groshen
,
Heinz - Josef Lenz
,
Robert D. Ladner
BMC Medical Genomics
2009
Despite the significant progress made in colon cancer chemotherapy, advanced disease remains largely incurable and novel…Â
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2007
2007
Effect of the histone deacetylase inhibitor LBH589 against epidermal growth factor receptor-dependent human lung cancer cells.
Arthur Edwards
,
Jiannong Li
,
Peter W Atadja
,
Kapil Bhalla
,
Eric B. Haura
Molecular cancer therapeutics
2007
Activating mutations in the epidermal growth factor receptor (EGFR) selectively activate signal transducers and activators of…Â
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Highly Cited
2006
Highly Cited
2006
The histone deacetylase inhibitor LBH589 is a potent antimyeloma agent that overcomes drug resistance.
Patricia Maiso
,
Xonia Carvajal-Vergara
,
+6 authors
Jesús Fernando San Miguel
Cancer research
2006
Multiple myeloma represents an incurable disease, for which development of new therapies is required. Here, we report the effect…Â
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Highly Cited
2006
Highly Cited
2006
Targeting tumor angiogenesis with histone deacetylase inhibitors: the hydroxamic acid derivative LBH589.
David Z. Qian
,
Yukihiko Kato
,
+6 authors
Roberto Pili
Clinical cancer research : an official journal of…
2006
PURPOSE Angiogenesis is required for tumor progression and represents a rational target for therapeutic intervention. Histone…Â
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Highly Cited
2006
Highly Cited
2006
A phase I study of intravenous LBH589, a novel cinnamic hydroxamic acid analogue histone deacetylase inhibitor, in patients with refractory hematologic malignancies.
Francis J Giles
,
Thomas Fischer
,
+11 authors
Kapil Bhalla
Clinical cancer research : an official journal of…
2006
PURPOSE LBH589 is a novel histone deacetylase inhibitor that inhibits proliferation and induces apoptosis in tumor cell lines. In…Â
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Highly Cited
2006
Highly Cited
2006
Aggresome induction by proteasome inhibitor bortezomib and alpha-tubulin hyperacetylation by tubulin deacetylase (TDAC) inhibitor LBH589 are synergistic in myeloma cells.
Laurence P. Catley
,
Ellen Weisberg
,
+8 authors
Kenneth C. Anderson
Blood
2006
Histone deacetylase (HDAC) inhibitors have shown cytotoxicity as single agents in preclinical studies for multiple myeloma (MM…Â
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Highly Cited
2006
Highly Cited
2006
Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer.
Ling Geng
,
Kyle C. Cuneo
,
Allie Fu
,
Tianxiang Tu
,
Peter W Atadja
,
Dennis E. Hallahan
Cancer research
2006
Histone deacetylases (HDAC) have been identified as therapeutic targets due to their regulatory function in DNA structure and…Â
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Highly Cited
2005
Highly Cited
2005
Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3.
Prince George
,
Purva Bali
,
+8 authors
Kapil Bhalla
Blood
2005
Present studies show that LBH589, a novel cinnamic hydroxamic acid analog histone deacetylase inhibitor, induces acetylation of…Â
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Highly Cited
2005
Highly Cited
2005
Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors.
Purva Bali
,
Michael Pranpat
,
+9 authors
Kapil Bhalla
The Journal of biological chemistry
2005
The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs) LAQ824 and LBH589 have been shown to induce…Â
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