Journal article
Catalytic properties of ADAM12 and its domain deletion mutants.
- Abstract:
-
Human ADAM12 (a disintegrin and metalloproteinase) is a multidomain zinc metalloproteinase expressed at high levels during development and in human tumors. ADAM12 exists as two splice variants: a classical type 1 membrane-anchored form (ADAM12-L) and a secreted splice variant (ADAM12-S) consisting of pro, catalytic, disintegrin, cysteine-rich, and EGF domains. Here we present a novel activity of recombinant ADAM12-S and its domain deletion mutants on S-carboxymethylated transferrin (Cm-Tf). C...
Expand abstract
- Publication status:
- Published
Actions
Access Document
- Publisher copy:
- 10.1021/bi701629c
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Bibliographic Details
- Journal:
- Biochemistry
- Volume:
- 47
- Issue:
- 2
- Pages:
- 537-547
- Publication date:
- 2008-01-01
- DOI:
- EISSN:
-
1520-4995
- ISSN:
-
0006-2960
- Source identifiers:
-
226364
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:226364
- UUID:
-
uuid:546ce600-247f-4802-91b2-482adca18c6d
- Local pid:
- pubs:226364
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2008
If you are the owner of this record, you can report an update to it here: Report update to this record