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Crystal Structure of the Central Coiled-Coil Domain from Human Liprin-β2Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 ReceptorEvolution and divergence of the mammalian SAMD9/SAMD9L gene familySterile alpha motif containing 7 (samd7) is a novel crx-regulated transcriptional repressor in the retina.A human sterile alpha motif domain polymerizome.Three Drosophila liprins interact to control synapse formation.A SAM oligomerization domain shapes the genomic binding landscape of the LEAFY transcription factorBicc1 Polymerization Regulates the Localization and Silencing of Bound mRNA.Expression and localization of sterile alpha motif domain containing 5 is associated with cell type and malignancy of biliary treeNMR structure of a heterodimeric SAM:SAM complex: characterization and manipulation of EphA2 binding reveal new cellular functions of SHIP2.Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insightsSLP-76 sterile α motif (SAM) and individual H5 α helix mediate oligomer formation for microclusters and T-cell activation.Three proteins mediate import of transit sequence-less precursors into the inner envelope of chloroplasts in Arabidopsis thaliana.Genomic and biochemical insights into the specificity of ETS transcription factors.New functions of the chloroplast Preprotein and Amino acid Transporter (PRAT) family members in protein import.Tankyrases: structure, function and therapeutic implications in cancer.Human polyhomeotic homolog 3 (PHC3) sterile alpha motif (SAM) linker allows open-ended polymerization of PHC3 SAM.The growth-suppressive function of the polycomb group protein polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domainStructural insights into SAM domain-mediated tankyrase oligomerization.The PNT domain from Drosophila pointed-P2 contains a dynamic N-terminal helix preceded by a disordered phosphoacceptor sequence.HP30-2, a mitochondrial PRAT protein for import of signal sequence-less precursor proteins in Arabidopsis thaliana.CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.
P2860
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P2860
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Identifying polymer-forming SAM domains.
@en
Identifying polymer-forming SAM domains.
@nl
type
label
Identifying polymer-forming SAM domains.
@en
Identifying polymer-forming SAM domains.
@nl
prefLabel
Identifying polymer-forming SAM domains.
@en
Identifying polymer-forming SAM domains.
@nl
P2860
P356
P1433
P1476
Identifying polymer-forming SAM domains.
@en
P2093
Alejandro D Meruelo
James U Bowie
P2860
P356
10.1002/PROT.22232
P407
P577
2009-01-01T00:00:00Z