Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3 (Q27684571)

5

object named as

James U Bowie

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author name string

Catherine N Leettola

1

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Mary Jane Knight

2

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Sigrid Hoffman

describes a project that uses

4

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publication date

7 July 2014

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published in

BMC Structural Biology

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volume

14

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issue

1

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page(s)

17

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ImageJ

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC4105859/fullTextXML

inferred from PubMed Central ID database lookup

exact match

https://scigraph.springernature.com/pub.10.1186/1472-6807-14-17

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cites work

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The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam

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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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Regulation of enzyme localization by polymerization: polymer formation by the SAM domain of diacylglycerol kinase delta1

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

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A human sterile alpha motif domain polymerizome

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Transgenic overexpression of Anks6(p.R823W) causes polycystic kidney disease in rats

29 September 2017

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29 September 2017

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Identifiers

DOI

10.1186/1472-6807-14-17

1 reference

Dimensions Publication ID

3958322

1023195926

0 references

3958322

1 reference

1 reference

1 reference