Zobrazeno 1 - 10
of 210
pro vyhledávání: '"Ida J. van der Klei"'
Autor:
Fei Wu, Ida J. van der Klei
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 10 (2022)
In the yeast Hansenula polymorpha, the ER protein Pex32 is required for associating peroxisomes to the ER. Here, we report on a structure–function analysis of Pex32. Localization studies of various Pex32 truncations showed that the N-terminal trans
Externí odkaz:
https://doaj.org/article/487ac996ebf54dcab0a51ea0f4ff71cd
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 10 (2022)
In the yeast Hansenula polymorpha the peroxisomal membrane protein Pex11 and three endoplasmic reticulum localized proteins of the Pex23 family (Pex23, Pex24 and Pex32) are involved in the formation of peroxisome-ER contact sites. Previous studies su
Externí odkaz:
https://doaj.org/article/defab6b8582e4cc5b454f464b4073143
Autor:
Renate L. M. Jansen, Carlos Santana-Molina, Marco van den Noort, Damien P. Devos, Ida J. van der Klei
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
PEX genes encode proteins involved in peroxisome biogenesis and proliferation. Using a comparative genomics approach, we clarify the evolutionary relationships between the 37 known PEX proteins in a representative set of eukaryotes, including all com
Externí odkaz:
https://doaj.org/article/f732ca56e6b04c6fbe620612bf9be072
Publikováno v:
Contact, Vol 3 (2020)
Saccharomyces cerevisiae Vac8 is a vacuolar membrane protein, which functions in vacuole inheritance and fusion, nucleus-vacuole junctions, autophagy and the cytoplasm-to-vacuole-targeting pathway. Here, we analyzed Vac8 of the yeast Hansenula polymo
Externí odkaz:
https://doaj.org/article/bc38c272cc8641e69f9db9a8ca3a33f6
Autor:
Huala Wu, Ida J. van der Klei
Publikováno v:
Contact, Vol 2 (2019)
Peroxisomes are important organelles and present in almost all eukaryotic cells. Close associations between peroxisomes and other cell compartments are known for several decades. The first molecular details of physical contacts between peroxisomes an
Externí odkaz:
https://doaj.org/article/19a8cc02ed874b279a3f26aa378c5895
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 16, p 4023 (2019)
There is an ongoing debate on how peroxisomes form: by growth and fission of pre-existing peroxisomes or de novo from another membrane. It has been proposed that, in wild type yeast cells, peroxisome fission and careful segregation of the organelles
Externí odkaz:
https://doaj.org/article/9da0a9864dc1431dad9ede7a903b46d7
Autor:
Adam Kawałek, Ida J. van der Klei
Publikováno v:
Microbial Cell, Vol 1, Iss 6, Pp 189-202 (2014)
Dietary restriction is generally assumed to increase the lifespan in most eukaryotes, including the simple model organism Saccharomyces cerevisiae. However, recent data questioned whether this phenomenon is indeed true for yeast. We studied the effec
Externí odkaz:
https://doaj.org/article/81356d538c5d47d2bfbc36b7e42947ab
Autor:
Marten Veenhuis, Ida J. van der Klei
Publikováno v:
Microbial Cell, Vol 1, Iss 4, Pp 128-130 (2014)
We describe an alternative peroxisome formation pathway in yeast pex3 and pex19 cells, which relies on the existence of small peroxisomal remnants that are present in these cells. This groundbreaking result challenges current models prescribing that
Externí odkaz:
https://doaj.org/article/bf564bc318d9470c9a90aa73147359e9
Autor:
Joël R. Roelofsen, Denis Martinez, Alwin M. Hartman, Anna K. H. Hirsch, Marc Bramkamp, Abigail Savietto, Anabela de Sousa Borges, Birgit Habenstein, Ida J. van der Klei, Aleksandra Zielińska, Rinse de Boer, Mélanie Berbon, Dirk-Jan Scheffers
Publikováno v:
eLife
International
England
eLife, Vol 9 (2020)
eLife, 9:e57179, 1-21. ELIFE SCIENCES PUBLICATIONS LTD
International
England
eLife, Vol 9 (2020)
eLife, 9:e57179, 1-21. ELIFE SCIENCES PUBLICATIONS LTD
The bacterial plasma membrane is an important cellular compartment. In recent years it has become obvious that protein complexes and lipids are not uniformly distributed within membranes. Current hypotheses suggest that flotillin proteins are require
Autor:
Ritika Singh, Selvambigai Manivannan, Arjen M Krikken, Damien P. Devos, Rinse de Boer, Nicola Bordin, Ida J. van der Klei
Publikováno v:
The FEBS Journal, 287(9), 1742-1757. NLM (Medline)
Digital.CSIC. Repositorio Institucional del CSIC
instname
The Febs Journal
Digital.CSIC. Repositorio Institucional del CSIC
instname
The Febs Journal
Here, we describe a novel peroxin, Pex37, in the yeast Hansenula polymorpha. H. polymorpha Pex37 is a peroxisomal membrane protein, which belongs to a protein family that includes, among others, the Neurospora crassa Woronin body protein Wsc, the hum