OmicsDI
Toggle navigation
Browse
Submit Data
Databases
API
Help
Advanced
Search
2
Results
Show all
Save search
Copy query
Show results for
Unknown
(1)
Proteomics
(1)
Organisms
Alphavirus
(1)
Anemia
(1)
Betaherpesvirinae
(1)
Brassica oleracea var. oleracea
(1)
Cowpox virus
(1)
Coxsackievirus
(1)
Cytomegalovirus
(1)
Dengue virus
(1)
EFO:0001352
(1)
Filoviridae
(1)
Hepatitis B virus
(1)
Human alphaherpesvirus 1
(1)
Human betaherpesvirus 5
(1)
Human immunodeficiency virus
(1)
Human immunodeficiency virus 1
(1)
Human immunodeficiency virus 2
(1)
Influenza A virus
(1)
Influenza C virus
(1)
Japanese encephalitis virus
(1)
Japanese encephalitis virus group
(1)
Lyssavirus rabies
(1)
Monkeypox virus
(1)
Orthopoxvirus
(1)
Orthopoxvirus vaccinia
(1)
Rattus
(1)
Ruditapes decussatus
(1)
Staphylococcus aureus
(1)
Tick-borne encephalitis virus
(1)
Viruses
(1)
West Nile virus
(1)
Repository
pride
(1)
Tissue
Cell culture
(1)
Epithelial cell
(1)
Kidney
(1)
Technology Type
Gel-based experiment
(1)
Mass Spectrometry
(1)
Shotgun proteomics
(1)
Publication Date
2020
(1)
Release Date
2017
(1)
Lab affiliation
Wellcome Centre for Cell-Matrix Research, Division of Cell-Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology Medicine and Health, The University of Manchester, Manchester Academic Health Science Centre, Manchester, UK
(1)
Previous
page
1 / 1
You're on page
1
Next
page
Sort
by:
Relevance
Page size
10
Prion protein facilitates retinal iron uptake and is cleaved at the β-site: Implications for retinal iron homeostasis in prion disorders.
Not available
S-EPMC5575325
|
biostudies-literature
Cite
Integrin adhesion complexes formed on different basement membrane ligands
Adhesion complexes isolated from cells in culture. Podocytes were attached to different extracellular matrix ligands and adhesion complex isolated.
ORGANISM(S):
Homo sapiens (Human)
2020-03-09
|
PXD017913
|
Pride
Podocyte
Ab
Extracellular matrix ligand.
Integrins
Adhesions
Rpe19
Cite
Previous
page
1 / 1
You're on page
1
Next
page
Sort
by:
Relevance
Page size
10
OmicsDI
is part of the ELIXIR infrastructure
OmicsDI is an Elixir interoperability service.
Learn more ›
Tweets