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Siah2-dependent concerted activity of HIF and FoxA2 regulates formation of neuroendocrine phenotype and neuroendocrine prostate tumorsStructure-Based Design of Covalent Siah InhibitorsTwo high-resolution structures of the human E3 ubiquitin ligase Siah1Fine tuning of the UPR by the ubiquitin ligases Siah1/2.Anti-CD73 antibody therapy inhibits breast tumor growth and metastasis.Distinct expression patterns of the E3 ligase SIAH-1 and its partner Kid/KIF22 in normal tissues and in the breast tumoral processes.Siah ubiquitin ligases modulate nodal signaling during zebrafish embryonic developmentThe ubiquitin ligase Siah2 and the hypoxia response.Inhibition of Siah2 ubiquitin ligase by vitamin K3 (menadione) attenuates hypoxia and MAPK signaling and blocks melanoma tumorigenesisSe-methylselenocysteine sensitizes hypoxic tumor cells to irinotecan by targeting hypoxia-inducible factor 1alpha.The Ski protein negatively regulates Siah2-mediated HDAC3 degradationThe antioxidant N-acetylcysteine prevents HIF-1 stabilization under hypoxia in vitro but does not affect tumorigenesis in multiple breast cancer models in vivo.The expression of the ubiquitin ligase SIAH2 (seven in absentia homolog 2) is mediated through gene copy number in breast cancer and is associated with a basal-like phenotype and p53 expressionHerpes simplex virus immediate-early protein ICP0 is targeted by SIAH-1 for proteasomal degradation.The ubiquitin ligase Siah is a novel regulator of Zeb1 in breast cancer.The Expression of the Ubiquitin Ligase SIAH2 (Seven In Absentia Homolog 2) Is Increased in Human Lung Cancer.Suppression of cell migration is promoted by miR-944 through targeting of SIAH1 and PTP4A1 in breast cancer cells.E3 ubiquitin ligases SIAH1/2 regulate hypoxia-inducible factor-1 (HIF-1)-mediated Th17 cell differentiation.SIAH2 protein expression in breast cancer is inversely related with ER status and outcome to tamoxifen therapyHypoxia-inducible factor prolyl-4-hydroxylase PHD2 protein abundance depends on integral membrane anchoring of FKBP38.Targeting the hypoxia-inducible factor (HIF) pathway in cancer.The Siah2-HIF-FoxA2 axis in prostate cancer – new markers and therapeutic opportunities.Regulators and effectors of Siah ubiquitin ligases.The role and therapeutic implications of RING-finger E3 ubiquitin ligases in hepatocellular carcinoma.Phylogenetic analysis of the SINA/SIAH ubiquitin E3 ligase family in Metazoa.SIAH ubiquitin ligases regulate breast cancer cell migration and invasion independent of the oxygen status.Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic signaling pathways.Nuclear accumulation of seven in absentia homologue-2 supports motility and proliferation of liver cancer cells.Siah2 regulates tight junction integrity and cell polarity through control of ASPP2 stability.Exosomal miR-141-3p regulates osteoblast activity to promote the osteoblastic metastasis of prostate cancer.Siah2-deficient mice show impaired skin wound repair.Testing the Effects of SIAH Ubiquitin E3 Ligases on Lysine Acetyl Transferases.A New Strategy to Control and Eradicate "Undruggable" Oncogenic K-RAS-Driven Pancreatic Cancer: Molecular Insights and Core Principles Learned from Developmental and Evolutionary BiologyBreast Cancer-Derived Exosomes Alter Macrophage Polarization via gp130/STAT3 Signaling.
P2860
Q24337932-9E89CC20-73FB-425B-9BFE-9A33531C5747Q27679208-6493254A-0785-4C6F-B5D6-16AC44FD93A7Q27680823-18421A6F-B77C-448D-850D-DE34A0C97815Q33583668-E2A0DE70-661B-454D-8BE9-FB17B330BDE2Q33667612-993E9B9F-F462-4FCD-A98F-3A8121E113B9Q33702293-86D28CEB-0E8A-444E-8B89-45F3575D865AQ33707971-A4C0E828-C4C1-4C05-AD57-88AF09EFBF0BQ33813039-7544B84A-80B0-476E-A23C-ADDC8FF90EACQ33825403-2FD28C53-7684-4183-A53A-277136047FF7Q34047866-75215041-D7E6-499D-8CE5-DC8043E2023CQ34133144-ACE5347E-01D6-445C-9A76-802487B20388Q34805346-6372300F-42B3-48B6-AB86-0E21E4F20BA8Q35029589-CD6FB8EE-31E5-4874-BA5A-E6D5B4823A60Q35140332-73786852-69BA-4ECC-AE47-854E1FE28170Q35176165-629E6F9B-3421-41AD-88C3-01E30F073BB2Q35845192-D907AAEC-20CF-4C68-9E7C-B46EB08FFC5BQ36067663-68B4C254-9788-4221-A2CA-4C27057CB887Q36321913-8673FEDF-A153-4E54-988B-04C1C4B34804Q36878697-211D2D77-3C6F-454E-942B-5DAC5289E954Q37371723-64FF11CC-19D4-4ACE-8B7C-949E31874492Q37587446-07135B11-BDF3-40A3-B447-BF8CA16A723AQ37805340-7058E499-363F-44A9-9FC5-C675034227FAQ38108753-6C45651E-5D13-41E8-9751-949760EC284EQ38178169-8224BC90-7A22-416C-8843-DB91642E6BC0Q38636574-3AD68A68-3075-4941-BBA5-80A47DADF5D0Q38812815-2FFC9BFA-F3F2-46DF-9776-63362433B534Q39300074-D1D79DAC-2931-4F4D-9752-B9551579EEA1Q39398502-BE003CCB-B28B-4176-A456-FA2FAED9519EQ41933303-717CE55C-AD1E-4731-9A5E-B3F3265E89B7Q47158987-B9D23976-DCBD-4311-A57C-A9082F3BA8A2Q51032620-FF992901-0F84-4B7C-A7BD-1CA9EDAFF08BQ51373926-5FE8D34E-B0D5-42DE-8CF2-AD110FF58D13Q54989340-EF48B21B-89B1-4EDD-9DF3-B5235DBB9B4BQ55308550-9614ECC6-5782-46ED-BB2D-9AA9AA7F81D8
P2860
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Inhibition of Siah ubiquitin ligase function.
@ast
Inhibition of Siah ubiquitin ligase function.
@en
Inhibition of Siah ubiquitin ligase function.
@nl
type
label
Inhibition of Siah ubiquitin ligase function.
@ast
Inhibition of Siah ubiquitin ligase function.
@en
Inhibition of Siah ubiquitin ligase function.
@nl
prefLabel
Inhibition of Siah ubiquitin ligase function.
@ast
Inhibition of Siah ubiquitin ligase function.
@en
Inhibition of Siah ubiquitin ligase function.
@nl
P2093
P2860
P356
P1433
P1476
Inhibition of Siah ubiquitin ligase function
@en
P2093
P2860
P2888
P304
P356
10.1038/ONC.2008.382
P407
P577
2008-10-13T00:00:00Z
P5875
P6179
1006482484