First-pass extracted concept

type III human CD38

Candidate: toolkit item1 source documents4 linked claims

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Evidence Snippets

CD38 can also exist in an opposite type III orientation with its catalytic domain facing the cytosol.

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1primary paper2017Proceedings of the National Academy of SciencesDOI PubMed

1 evidence snippet 4 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1functional activitysupports2017Source 1DOI PubMed

Type III CD38 is functionally active in producing cellular cADPR and this activity is specifically modulated through interaction with cytosolic CIB1.

Quoted textsource-backed

The results indicate that the type III CD38 is functionally active in producing cellular cADPR and that the activity is specifically modulated through interaction with cytosolic CIB1.

Claim 2interaction mappingsupports2017Source 1DOI PubMed

The N terminus of CIB1 is the interacting domain for CD38 binding.

Quoted textsource-backed

Mutational studies established that the N terminus of CIB1 is the interacting domain.

Claim 3occurrence in cellssupports2017Source 1DOI PubMed

Type III CD38 is naturally occurring in human multiple myeloma cells.

Quoted textsource-backed

firmly established that it is naturally occurring in human multiple myeloma cells

Claim 4protein interactionsupports2017Source 1DOI PubMed

CIB1 binds specifically to the catalytic domain of CD38.

Quoted textsource-backed

The results from immunoprecipitation, ELISA, and bimolecular fluorescence complementation confirmed that CIB1 binds specifically to the catalytic domain of CD38, in vivo and in vitro.