Léim chuig an ábhar
VuFind
English
Deutsch
Español
Français
Italiano
日本語
Nederlands
Português
Português (Brasil)
中文(简体)
中文(繁體)
Türkçe
עברית
Gaeilge
Cymraeg
Ελληνικά
Català
Euskara
Русский
Čeština
Suomi
Svenska
polski
Dansk
slovenščina
اللغة العربية
বাংলা
Galego
Tiếng Việt
Hrvatski
हिंदी
Հայերէն
Українська
Sámegiella
Монгол
Teanga
Gach réimse
Teideal
Údar
Ábhar
Gairmuimhir
ISBN/ISSN
Clib
AIMSIGH
CASTA
Investigation of the endocytic...
Luaigh é seo
Seol mar théacs é seo
Seol é seo mar r-phost
Priontáil
Easpórtáil taifead
Easpórtáil chuig RefWorks
Easpórtáil chuig EndNoteWeb
Easpórtáil chuig EndNote
Buan-nasc
Investigation of the endocytic pathway of ADAMTS-4
Sonraí bibleagrafaíochta
Príomhchruthaitheoirí:
Owen, K
,
Troeberg, L
,
Parker, A
,
Nagase, H
Formáid:
Journal article
Foilsithe / Cruthaithe:
2009
Stoc
Cur síos
Míreanna comhchosúla
Amharc foirne
Míreanna comhchosúla
Low density lipoprotein receptor-related protein 1 (LRP1)-mediated endocytic clearance of a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4): functional differences of non-catalytic domains of ADAMTS-4 and ADAMTS-5 in LRP1 binding.
de réir: Yamamoto, K, et al.
Foilsithe / Cruthaithe: (2014)
Endocytic pathways of TIMP-3 and its N-terminal inhibitory domain
de réir: Scilabra, S, et al.
Foilsithe / Cruthaithe: (2009)
Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity.
de réir: Fushimi, K, et al.
Foilsithe / Cruthaithe: (2008)
MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1
de réir: Yamamoto, K, et al.
Foilsithe / Cruthaithe: (2016)
The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.
de réir: Troeberg, L, et al.
Foilsithe / Cruthaithe: (2009)