NMR structure of a heterodimeric SAM:SAM complex: characterization and manipulation of EphA2 binding reveal new cellular functions of SHIP2. (Q36451527)

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English	NMR structure of a heterodimeric SAM:SAM complex: characterization and manipulation of EphA2 binding reveal new cellular functions of SHIP2.	scientific article

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scholarly article

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Europe PubMed Central

PMC publication ID

14 August 2017

NMR structure of a heterodimeric SAM:SAM complex: characterization and manipulation of EphA2 binding reveal new cellular functions of SHIP2. (English)

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Europe PubMed Central

PMC publication ID

14 August 2017

Prasanta K Hota

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Prasanta K Hota

2

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Matthias Buck

10

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author name string

Hyeong J Lee

1

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Europe PubMed Central

PMC publication ID

14 August 2017

Preeti Chugha

3

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Europe PubMed Central

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14 August 2017

Hong Guo

4

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Europe PubMed Central

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14 August 2017

Hui Miao

5

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Europe PubMed Central

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14 August 2017

Liqun Zhang

6

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Europe PubMed Central

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14 August 2017

Soon-Jeung Kim

7

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Europe PubMed Central

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14 August 2017

Lukas Stetzik

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Europe PubMed Central

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14 August 2017

Bing-Cheng Wang

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14 August 2017

publication date

1 January 2012

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Europe PubMed Central

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14 August 2017

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Europe PubMed Central

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14 August 2017

20

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Europe PubMed Central

PMC publication ID

14 August 2017

1

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Europe PubMed Central

PMC publication ID

14 August 2017

41-55

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Europe PubMed Central

PMC publication ID

14 August 2017

All-atom empirical potential for molecular modeling and dynamics studies of proteins

1 reference

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A simultaneous (15)N, (1)H- and (13)C, (1)H-HSQC with sensitivity enhancement and a heteronuclear gradient echo

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Challenge of large-scale motion for residual dipolar coupling based analysis of configuration: the case of fibrosterol sulfate A.

1 reference

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The membrane bound LRR lipoprotein Slr, and the cell wall-anchored M1 protein from Streptococcus pyogenes both interact with type I collagen

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1 reference

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EphA2 mediates ligand-dependent inhibition and ligand-independent promotion of cell migration and invasion via a reciprocal regulatory loop with Akt

1 reference

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NMR Studies of a Heterotypic Sam−Sam Domain Association: The Interaction between the Lipid Phosphatase Ship2 and the EphA2 Receptor † , ‡

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CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling

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Scalable molecular dynamics with NAMD

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The many faces of SAM

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Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: implications for efficient signaling through the MAPK cascades

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EphA kinase activation regulates HGF-induced epithelial branching morphogenesis

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Native interface of the SAM domain polymer of TEL.

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30 September 2017

The SAM domain of polyhomeotic forms a helical polymer

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Mapping protein-protein interactions in solution by NMR spectroscopy

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Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel.

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Activation of EphA receptor tyrosine kinase inhibits the Ras/MAPK pathway

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Monomeric structure of the human EphB2 sterile alpha motif domain

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Oligomeric structure of the human EphB2 receptor SAM domain

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10.1016/J.STR.2011.11.013

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Europe PubMed Central

PMC publication ID

14 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PubMed publication ID

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Europe PubMed Central

PMC publication ID

14 August 2017

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