Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation. - Wikidata - awgldk - TriplyDB

Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

http://www.wikidata.org/entity/Q34578847

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Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1 Nucleosome-interacting proteins regulated by DNA and histone methylation Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1 Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes Keeping it in the family: diverse histone recognition by conserved structural folds A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption.The Tudor domain protein Spindlin1 is involved in intrinsic antiviral defense against incoming hepatitis B Virus and herpes simplex virus type 1 AIP1 is a novel Agenet/Tudor domain protein from Arabidopsis that interacts with regulators of DNA replication, transcription and chromatin remodeling.Structure and function of histone methylation binding proteins.SSTY proteins co-localize with the post-meiotic sex chromatin and interact with regulators of its expression.Tudor: a versatile family of histone methylation 'readers'.Mind the methyl: methyllysine binding proteins in epigenetic regulation.Molecular basis underlying the biological effects elicited by extremely low-frequency magnetic field (ELF-MF) on neuroblastoma cells.Suppression of SPIN1-mediated PI3K-Akt pathway by miR-489 increases chemosensitivity in breast cancer.The histone code reader SPIN1 controls RET signaling in liposarcoma.Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions.Comparative Interactomes of VRK1 and VRK3 with Their Distinct Roles in the Cell Cycle of Liver Cancer A transcriptional coregulator, SPIN·DOC, attenuates the coactivator activity of Spindlin1.SPIN1 is a proto-oncogene and SPIN3 is a tumor suppressor in human seminoma

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P2860

Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

http://www.wikidata.org/entity/Q34578847

description

2006 nî lūn-bûn

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2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

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Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation.

@en

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Beili Wu

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

Cixian Bai

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Feng Xu

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Fuguo Jiang

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Hongfeng Yuan

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

Lipeng Qin

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

Mark Bartlam

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

Qiang Zhao

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Wen Yue

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Xiaoyan Xie

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface

ESPript: analysis of multiple sequence alignments in PostScript

SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets

Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

Functional cloning of SPIN-2, a nuclear anti-apoptotic protein with roles in cell cycle progression.

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647-656

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scholarly article

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10.1074/JBC.M604029200

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282

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2006-11-01T00:00:00Z

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