about
Probing the in vivo function of Mad1:C-Mad2 in the spindle assembly checkpointChemical Structure-Biological Activity Models for Pharmacophores' 3D-InteractionsThe multifaceted roles of the HORMA domain in cellular signalingA role of WT1 in cell division and genomic stabilityStructural Basis of Recruitment of DNA Polymerase by Interaction between REV1 and REV7 ProteinsMutational Tipping Points for Switching Protein Folds and FunctionsStructure of the mitotic checkpoint complexStructure of human Mad1 C-terminal domain reveals its involvement in kinetochore targetingStructure of the Atg101-Atg13 complex reveals essential roles of Atg101 in autophagy initiationA designed point mutant in Fis1 disrupts dimerization and mitochondrial fissionThe transcription factor TFII-I promotes DNA translesion synthesis and genomic stabilityVirtual screening on an α-helix to β-strand switchable region of the FGFR2 extracellular domain revealed positive and negative modulators.Structural gymnastics of multifunctional metamorphic proteins.Molecular dynamics simulation on the conformational transition of the mad2 protein from the open to the closed state.Removal of Spindly from microtubule-attached kinetochores controls spindle checkpoint silencing in human cellsA nuclear magnetic resonance based approach to accurate functional annotation of putative enzymes in the methanogen Methanosarcina acetivorans.Disassembly of mitotic checkpoint complexes by the joint action of the AAA-ATPase TRIP13 and p31(comet).Proteins that switch foldsThyroid hormone receptor interacting protein 13 (TRIP13) AAA-ATPase is a novel mitotic checkpoint-silencing proteinWT1 interacts with MAD2 and regulates mitotic checkpoint functionThe dynamics of signal amplification by macromolecular assemblies for the control of chromosome segregationPhosphorylation of the spindle checkpoint protein Mad2 regulates its conformational transition.Bimodal activation of BubR1 by Bub3 sustains mitotic checkpoint signalingp31comet Promotes disassembly of the mitotic checkpoint complex in an ATP-dependent processStructure-biological function relationship extended to mitotic arrest-deficient 2-like protein Mad2 native and mutants-new opportunity for genetic disorder control.The Cdc20-binding Phe box of the spindle checkpoint protein BubR1 maintains the mitotic checkpoint complex during mitosis.BUBR1 and closed MAD2 (C-MAD2) interact directly to assemble a functional mitotic checkpoint complex.A mad partner for Shugoshin in meiosis.Defining pathways of spindle checkpoint silencing: functional redundancy between Cdc20 ubiquitination and p31(comet)Mutual regulation between the spindle checkpoint and APC/C.Closed MAD2 (C-MAD2) is selectively incorporated into the mitotic checkpoint complex (MCC)Structure of an intermediate conformer of the spindle checkpoint protein Mad2Making an effective switch at the kinetochore by phosphorylation and dephosphorylation.Smurf2 as a novel mitotic regulator: From the spindle assembly checkpoint to tumorigenesisEnhanced genomic instabilities caused by deregulated microtubule dynamics and chromosome segregation: a perspective from genetic studies in mice.Monopolar spindle 1 (MPS1) kinase promotes production of closed MAD2 (C-MAD2) conformer and assembly of the mitotic checkpoint complexA Bub1-Mad1 interaction targets the Mad1-Mad2 complex to unattached kinetochores to initiate the spindle checkpoint.Structure, function and mechanism of the anaphase promoting complex (APC/C).Bub1 and BubR1: at the interface between chromosome attachment and the spindle checkpointMonitoring the fidelity of mitotic chromosome segregation by the spindle assembly checkpoint.
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Protein metamorphosis: the two-state behavior of Mad2.
@en
Protein metamorphosis: the two-state behavior of Mad2.
@nl
type
label
Protein metamorphosis: the two-state behavior of Mad2.
@en
Protein metamorphosis: the two-state behavior of Mad2.
@nl
prefLabel
Protein metamorphosis: the two-state behavior of Mad2.
@en
Protein metamorphosis: the two-state behavior of Mad2.
@nl
P2860
P1433
P1476
Protein metamorphosis: the two-state behavior of Mad2.
@en
P2093
Hongtao Yu
Xuelian Luo
P2860
P304
P356
10.1016/J.STR.2008.10.002
P577
2008-11-01T00:00:00Z