Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Piia Vehviläinen"'
Autor:
Merja Lakso, Garry Wong, Martina Rudgalvyte, Merja Jaronen, Jari Koistinaho, Velta Keksa-Goldsteine, Michael J. Courtney, Šárka Lehtonen, Piia Vehviläinen, Gundars Goldsteins
Publikováno v:
Antioxidantsredox signaling. 25(8)
Protein misfolding occurs in neurodegenerative diseases, including Parkinson's disease (PD). In endoplasmic reticulum (ER), an overload of misfolded proteins, particularly alpha-synuclein (αSyn) in PD, may cause stress and activate the unfolded prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f81061d88c2efa114f25e9c9cf46cf5e
https://pubmed.ncbi.nlm.nih.gov/27139804
https://pubmed.ncbi.nlm.nih.gov/27139804
Autor:
Merja Jaronen, Tarja Malm, Jari Koistinaho, Piia Valonen, Gundars Goldsteins, Eveliina Pollari, Piia Vehviläinen, Velta Keksa-Goldsteine
Publikováno v:
Human Molecular Genetics. 22:646-655
Protein disulfide isomerase (PDI) is an oxidoreductase assisting oxidative protein folding in the endoplasmic reticulum of all types of cells, including neurons and glia. In neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), up
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25b1a56179710476838e1bbffe7f92ef
https://doi.org/10.1093/hmg/dds472
https://doi.org/10.1093/hmg/dds472
Publikováno v:
Journal of Cellular Physiology. 221:586-593
The components of the extracellular matrix (ECM) and their differential expression patterns play important roles in tissue formation. The deposition of latent TGF-beta binding proteins (LTBPs) to the ECM exhibit distinct distribution profiles. We hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a690257fbe3bab936ec3588191cfa61
https://doi.org/10.1002/jcp.21888
https://doi.org/10.1002/jcp.21888
Autor:
Juha Jäälinoja, Varpu Marjomäki, David E. Birk, Liisa Nissinen, Jyrki Heino, Mira Tulla, Leena Ala-Kokko, Petri Nykvist, Tiina Viitasalo, Joni Ylostalo, Richard W. Farndale, Jarmo Käpylä, Anna-Marja Säämänen, Piia Vehviläinen
Publikováno v:
Journal of Biological Chemistry. 279:51677-51687
Collagen IX is the prototype fibril-associated collagen with interruptions in triple helix. In human cartilage it covers collagen fibrils, but its putative cellular receptors have been unknown. The reverse transcription-PCR analysis of human fetal ti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68b8beef0a0f554f05c79ff2f5d73ee3
https://doi.org/10.1074/jbc.m409412200
https://doi.org/10.1074/jbc.m409412200
Autor:
Piia Vehviläinen, Johanna Jokinen, Hilkka Reunanen, Elina Dadu, Johanna Ivaska, Jarmo Käpylä, Jyrki Heino, Petri Nykvist, Lari Häkkinen, Daniel J. White, Hannu Larjava
Publikováno v:
Jokinen, J, Dadu, E, Nykvist, P, Käpylä, J, White, D J, Ivaska, J, Vehviläinen, P, Reunanen, H, Larjava, H, Häkkinen, L & Heino, J 2004, ' Integrin-mediated cell adhesion to type I collagen fibrils ', Journal of Biological Chemistry, vol. 279, no. 30, pp. 31956-31963 . https://doi.org/10.1074/jbc.M401409200
In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 and α2β1 integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I colla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcd87cd5b200c8ba648cadeadbdddbb3
https://doi.org/10.1074/jbc.m401409200
https://doi.org/10.1074/jbc.m401409200
Publikováno v:
Journal of Biological Chemistry. 278:24705-24713
Of the four latent transforming growth factor (TGF)-beta-binding proteins (LTBPs), LTBP-2 is different in the respect that it does not bind small latent forms of TGF-beta. LTBP-2 is therefore likely to have other roles in the extracellular matrix. LT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16634a016e17dad58f6741197b362907
https://doi.org/10.1074/jbc.m212953200
https://doi.org/10.1074/jbc.m212953200
Publikováno v:
Frontiers in Cellular Neuroscience, Vol 8 (2014)
Frontiers in Cellular Neuroscience
Frontiers in Cellular Neuroscience
In amyotrophic lateral sclerosis (ALS), mitochondrial dysfunction is recognized as one of the key elements contributing to the pathology. Mitochondria are the major source of intracellular reactive oxygen species (ROS). Increased production of ROS as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::073ee51e11ccf5acdd7979c87ae33d9c
Autor:
Pamela Lindholm, Katri Koli, Marjukka Myllärniemi, Vuokko L. Kinnula, Jorma Keski-Oja, Ylermi Soini, Kaisa Salmenkivi, Piia Vehviläinen
Publikováno v:
Human pathology. 42(2)
Malignant mesothelioma is an aggressive cancer of the pleura with poor prognosis. There is a need to identify new biomarkers and therapeutic targets for this invasive and fatal disease. Transforming growth factor β (TGF-β) can promote mesothelioma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b225839e58f75e721240d7d8c940ec7
https://pubmed.ncbi.nlm.nih.gov/21106222
https://pubmed.ncbi.nlm.nih.gov/21106222
Publikováno v:
Experimental cell research. 314(13)
Targeting of transforming growth factor beta (TGF-beta) to the extracellular matrix (ECM) by latent TGF-beta binding proteins (LTBPs) regulates the availability of TGF-beta for interactions with endothelial cells during their quiescence and activatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c571b4a4f62bf672986530c0809876b9
https://pubmed.ncbi.nlm.nih.gov/18602101
https://pubmed.ncbi.nlm.nih.gov/18602101
Publikováno v:
Antioxidantsredox signaling. 3(1)
Changes occur in gene expression during aging in vivo and in replicative senescence in vitro, suggesting that aging can affect gene regulation. We have recently observed age-related changes in ubiquitously expressed, oxidative stress-responsive nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d21814f44e7d5f5cca943d8ea201e00
https://pubmed.ncbi.nlm.nih.gov/11291593
https://pubmed.ncbi.nlm.nih.gov/11291593