Suberoylanilide hydroxamic acid (SAHA; vorinostat) causes bone loss by inhibiting immature osteoblasts. - Wikidata - awgldk - TriplyDB

Suberoylanilide hydroxamic acid (SAHA; vorinostat) causes bone loss by inhibiting immature osteoblasts.

Suberoylanilide hydroxamic acid (SAHA; vorinostat) causes bone loss by inhibiting immature osteoblasts.

http://www.wikidata.org/entity/Q34810920

about

Regulatory dendritic cells: there is more than just immune activation Histone deacetylase inhibitor MS-275 stimulates bone formation in part by enhancing Dhx36-mediated TNAP transcription Histone deacetylase 3 supports endochondral bone formation by controlling cytokine signaling and matrix remodeling.Runx2 is required for early stages of endochondral bone formation but delays final stages of bone repair in Axin2-deficient mice.Histone deacetylase inhibition destabilizes the multi-potent state of uncommitted adipose-derived mesenchymal stromal cells Deletion of histone deacetylase 7 in osteoclasts decreases bone mass in mice by interactions with MITF.Hdac-mediated control of endochondral and intramembranous ossification A Novel Osteogenic Activity of Suberoylanilide Hydroxamic Acid is Synergized by BMP-2.Histone Deacetylases in Bone Development and Skeletal Disorders.Histone deacetylase 3 is required for maintenance of bone mass during aging Histone Deacetylase Inhibitors Target the Leukemic Microenvironment by Enhancing a Nherf1-Protein Phosphatase 1α-TAZ Signaling Pathway in Osteoblasts Hdac3 Deficiency Increases Marrow Adiposity and Induces Lipid Storage and Glucocorticoid Metabolism in Osteochondroprogenitor Cells Runx2 protein represses Axin2 expression in osteoblasts and is required for craniosynostosis in Axin2-deficient mice Suberoylanilide hydroxamic acid represses glioma stem-like cells.Histone deacetylase inhibitors as suppressors of bone destruction in inflammatory diseases.Chromatin modifiers and histone modifications in bone formation, regeneration, and therapeutic intervention for bone-related disease.Epigenetic modulation of dental pulp stem cells: implications for regenerative endodontics.Enhancer of Zeste Homolog 2 Inhibition Stimulates Bone Formation and Mitigates Bone Loss Caused by Ovariectomy in Skeletally Mature Mice.Dynamic and distinct histone modifications of osteogenic genes during osteogenic differentiation.Histone Deacetylases in Cartilage Homeostasis and Osteoarthritis.Profiling of human epigenetic regulators using a semi-automated real-time qPCR platform validated by next generation sequencing.Effect of the HDAC inhibitor vorinostat on the osteogenic differentiation of mesenchymal stem cells in vitro and bone formation in vivo.Down-regulation of Sox11 is required for efficient osteogenic differentiation of adipose-derived stem cells Loss of Hdac3 in osteoprogenitors increases bone expression of osteoprotegerin, improving systemic insulin sensitivity.The Histone-Deacetylase-Inhibitor Suberoylanilide Hydroxamic Acid Promotes Dental Pulp Repair Mechanisms Through Modulation of Matrix Metalloproteinase-13 Activity.Histone deacetylase 3 suppresses Erk phosphorylation and matrix metalloproteinase (Mmp)-13 activity in chondrocytes.TGF-β1 impairs mechanosensation of human osteoblasts via HDAC6-mediated shortening and distortion of primary cilia.Histone deacetylase inhibitors reduce differentiating osteoblast-mediated protection of acute myeloid leukemia cells from cytarabine.Mesenchymal stem cells in multiple myeloma: a therapeutical tool or target?

P2860

Q28388235-CDC5AA0B-7E14-4C0D-9271-7DEEA5C75DD2 Q28505369-2410D5DF-E6A8-467C-97B8-CAB2EE7DB0B3 Q33614697-7E93AF20-E98E-41AC-B5E9-CEFFFA5DB11E Q34016769-CDB84068-92A0-406B-ADA8-A38B421A47BB Q34475885-40F439CF-C569-42A9-9A47-068695C4E108 Q35433533-A72DFE79-C386-4F36-9FE7-BB5BA246210F Q35556841-8A2F3DA7-8020-48EA-A0ED-F8BC695D85A9 Q35739595-880E4F7D-67EC-4E58-9013-482A451D1367 Q36146330-0E3072A5-7C91-4CC3-8C06-900246989870 Q36442972-658519A9-990F-4E94-8182-1266B694177B Q36444091-FF876EE5-4BB8-41A0-8A59-848CE20DC0DE Q36593452-02697434-2CA3-443B-99D0-BC810C584533 Q36635990-522D5923-2659-48CA-9C1D-FBBAF2EC20B1 Q37423898-55CFF751-AB67-49BC-8E7A-77FCC4BA596F Q38008692-A51E347A-FB7F-4EC2-A226-9766ADABDD09 Q38402465-4C328849-915E-453F-8DEC-6281809C14AB Q38502939-F799ED4C-4686-4198-A96F-004E6ACFFC7B Q38739722-D91A6ABB-032E-48D7-A2BA-D7F41B171D32 Q38863680-321869CE-432D-4456-A499-B3296C6671CA Q38893201-6BBE7BAA-C736-4D72-A952-155145B98004 Q38993135-BBB4EC9D-A340-4053-ABE8-E8BED584D2EE Q39020389-D2C8BEC3-AEF5-44BC-8A34-433A5E89E56E Q39303968-B9BDA00F-8EBC-4E4C-9BF9-D8AD617D4CBD Q42003109-CFAC6A70-57D1-4EC0-8ADD-D5870EB77454 Q46280254-B6D9A560-E109-445E-BD53-4B6955F3C9ED Q47105192-2700E3A2-B592-4A51-868B-A7209F1A9F47 Q48152374-DA9C37F9-51D4-4F91-96D3-6002CFAB7CE0 Q49167307-7339C27F-7282-4478-A4D5-14F27D21DE4E Q55471455-54BA4C61-F14E-4E24-97F3-8389298A1102

P2860

Suberoylanilide hydroxamic acid (SAHA; vorinostat) causes bone loss by inhibiting immature osteoblasts.

http://www.wikidata.org/entity/Q34810920

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Suberoylanilide hydroxamic aci ...... hibiting immature osteoblasts.

@ast

Suberoylanilide hydroxamic aci ...... hibiting immature osteoblasts.

@en

type

label

Suberoylanilide hydroxamic aci ...... hibiting immature osteoblasts.

@ast

Suberoylanilide hydroxamic aci ...... hibiting immature osteoblasts.

@en

prefLabel

Suberoylanilide hydroxamic aci ...... hibiting immature osteoblasts.

@ast

Suberoylanilide hydroxamic aci ...... hibiting immature osteoblasts.

@en

P1433

Q34810920-9D8E4C78-1ED4-4CAB-A6C5-9CF11F2CA686

P1476

Q34810920-7F8547C0-F944-4483-81BC-466D5962D7DC

P2093

Q34810920-29989255-B8B2-4700-9362-A1117D12C112

Q34810920-2DC2D36C-3443-4F6F-B31B-E6EBD6E727A1

Q34810920-3C52DFB2-6274-4A77-BD6C-0241667A9117

Q34810920-421DFE0A-90DA-4630-A9C3-A3167525A490

Q34810920-47E4A5DE-A046-48BE-8772-D26969E545EE

Q34810920-53F6B5F1-C410-473F-8A6B-3D1778140E70

Q34810920-5EB65ED1-6D44-4DA4-A426-4E11E5CC6834

Q34810920-704C757D-1146-4D47-AEF7-2D7333623F04

Q34810920-86AA16AE-D27D-4FFE-914C-20D50C4C3301

P2860

Q34810920-06B61D29-3DA1-4CA4-B1B9-BFB1EA0BB3F2

Q34810920-0C780E4F-1948-4521-89E6-C4FEEDADDD8F

Q34810920-0CE7BEAD-BACF-4AD3-8239-71BAF7A4CB6A

Q34810920-11043A2F-9C9A-4F3A-9E03-09B73F51206D

Q34810920-16FFFA49-296A-428B-B54A-9201D89F9ECC

Q34810920-1725DE47-6AC8-453A-B5FE-F5A0D08E5127

Q34810920-1757F747-BD56-4F76-94CE-40A2C0CBD6CD

Q34810920-1D2A0DBF-F4E3-4E42-9E35-B3055B9173F8

Q34810920-1DEC4507-ACF2-43DB-AE6C-22363AEF3387

Q34810920-1F78CCBB-DD4D-4F71-8AF5-E6967C0FEFC3

P304

Q34810920-A7DB98AE-499D-4564-B234-0AEDC7A450C3

P31

Q34810920-BA78A393-5B2F-426F-854F-0C5C77D777AE

P356

Q34810920-FB27BD96-CB2C-4203-A027-D8CFB486045C

P433

Q34810920-E1A79CEB-F371-4D1B-930B-A548223CEF69

P478

Q34810920-CE037FE3-73D4-4695-A286-C96E6F51F1BA

P50

Q34810920-241E31EC-CD39-4FA7-88ED-57672BC11C44

P577

Q34810920-7B22D242-F391-4A31-9952-F3C815D7CC5E

P5875

Q34810920-1664B23B-167F-4C02-B52C-E70BEECFB6B0

P698

Q34810920-0E30149A-370D-4E4C-9D4A-4CB22B5FEC4D

P921

Q34810920-113B685C-4348-4594-962E-FA6D83B8DE4F

P932

Q34810920-91D976F9-0F80-45F6-89DB-5C84FDE84B0D

P356

J.BONE.2011.01.007

P1433

P1476

Suberoylanilide hydroxamic aci ...... nhibiting immature osteoblasts

@en

P2093

Angela L McCleary-Wheeler

http://www.w3.org/2001/XMLSchema#string

Bridget A Stensgard

http://www.w3.org/2001/XMLSchema#string

David F Razidlo

http://www.w3.org/2001/XMLSchema#string

Frank J Secreto

http://www.w3.org/2001/XMLSchema#string

Gary S Stein

http://www.w3.org/2001/XMLSchema#string

Jane B Lian

http://www.w3.org/2001/XMLSchema#string

Jennifer J Westendorf

http://www.w3.org/2001/XMLSchema#string

Minzhi Zhang

http://www.w3.org/2001/XMLSchema#string

Xiaodong Li

http://www.w3.org/2001/XMLSchema#string

P2860

Histone deacetylases specifically down-regulate p53-dependent gene activation

Twenty bone-mineral-density loci identified by large-scale meta-analysis of genome-wide association studies

Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR

Histone deacetylase 7 associates with Runx2 and represses its activity during osteoblast maturation in a deacetylation-independent manner

Runx2 (Cbfa1, AML-3) interacts with histone deacetylase 6 and represses the p21(CIP1/WAF1) promoter

Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis

The many roles of histone deacetylases in development and physiology: implications for disease and therapy

Epigenetic control of skull morphogenesis by histone deacetylase 8

Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL)

Histone deacetylase 3 depletion in osteo/chondroprogenitor cells decreases bone density and increases marrow fat

P304

1117-1126

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.BONE.2011.01.007

http://www.w3.org/2001/XMLSchema#string

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

48

http://www.w3.org/2001/XMLSchema#string

P50

Meghan E McGee-Lawrence

P577

2011-01-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

49775033

http://www.w3.org/2001/XMLSchema#string

P698

21255693

http://www.w3.org/2001/XMLSchema#string

P921

P932

3079070

http://www.w3.org/2001/XMLSchema#string