(Q36451527)

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

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scholarly article

1 reference

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)

1 reference

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

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Preeti Chugha

3

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Europe PubMed Central

PMC publication ID

14 August 2017

Hong Guo

4

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Hui Miao

5

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Europe PubMed Central

PMC publication ID

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

PMC publication ID

14 August 2017

Lukas Stetzik

8

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Europe PubMed Central

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14 August 2017

Bing-Cheng Wang

9

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Europe PubMed Central

PMC publication ID

14 August 2017

publication date

1 January 2012

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Europe PubMed Central

PMC publication ID

14 August 2017

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

20

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Europe PubMed Central

PMC publication ID

14 August 2017

1

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

41-55

1 reference

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

1 reference

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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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1 reference

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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 † , ‡

1 reference

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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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Conformational changes associated with protein-protein interactions

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Ectopic EphA4 receptor induces posterior protrusions via FGF signaling in Xenopus embryos

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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.

1 reference

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The SAM domain of polyhomeotic forms a helical polymer

1 reference

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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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Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites

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Oligomeric structure of the human EphB2 receptor SAM domain

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The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization

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Distinct subdomains of the EphA3 receptor mediate ligand binding and receptor dimerization

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SAM as a protein interaction domain involved in developmental regulation

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10.1016/J.STR.2011.11.013

1 reference

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

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

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