Shedding of Collagen XVII/BP180: STRUCTURAL MOTIFS INFLUENCE CLEAVAGE FROM CELL SURFACE (Q29013483)

23 March 2017

author name string

C.-W. Franzke

1

1 reference

23 March 2017

K. Tasanen

2

1 reference

23 March 2017

L. Borradori

3

1 reference

23 March 2017

V. Huotari

4

1 reference

23 March 2017

L. Bruckner-Tuderman

5

1 reference

23 March 2017

language of work or name

English

0 references

publication date

26 March 2004

1 reference

Journal of Biological Chemistry

23 March 2017

published in

1 reference

23 March 2017

volume

279

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23 March 2017

issue

23

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23 March 2017

page(s)

24521-24529

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Type XIII collagen is identified as a plasma membrane protein

23 March 2017

cites work

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Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain

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Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15

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Properties of the Collagen Type XVII Ectodomain: EVIDENCE FOR N- TO C-TERMINAL TRIPLE HELIX FOLDING

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A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins

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Role of the Juxtamembrane Domains of the Transforming Growth Factor-α Precursor and the β-Amyloid Precursor Protein in Regulated Ectodomain Shedding

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21 January 2018

Identifiers

DOI

10.1074/JBC.M308835200

1 reference

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