Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Joseph L Costello"'
Autor:
Yunhong Wang, Jeremy Metz, Joseph L Costello, Josiah Passmore, Michael Schrader, Christian Schultz, Markus Islinger
Publikováno v:
PLoS ONE, Vol 13, Iss 12, p e0209507 (2018)
Peroxisomes can be frequently found in proximity to other subcellular organelles such as the endoplasmic reticulum (ER), mitochondria or lysosomes. The tail-anchored protein ACBD5 was recently identified as part of a tethering complex at peroxisome-E
Externí odkaz:
https://doaj.org/article/463161190464436ea07898e1c5226559
Autor:
Lydia M Castelli, David Talavera, Christopher J Kershaw, Sarah S Mohammad-Qureshi, Joseph L Costello, William Rowe, Paul F G Sims, Christopher M Grant, Simon J Hubbard, Mark P Ashe, Graham D Pavitt
Publikováno v:
PLoS Genetics, Vol 11, Iss 5, p e1005233 (2015)
Translation initiation factor eIF4E mediates mRNA selection for protein synthesis via the mRNA 5'cap. A family of binding proteins, termed the 4E-BPs, interact with eIF4E to hinder ribosome recruitment. Mechanisms underlying mRNA specificity for 4E-B
Externí odkaz:
https://doaj.org/article/4442571fc9da4cb6b3f3487cf8c78944
Autor:
Christopher J Kershaw, Joseph L Costello, Lydia M Castelli, David Talavera, William Rowe, Paul F G Sims, Mark P Ashe, Simon J Hubbard, Graham D Pavitt, Chris M Grant
Publikováno v:
PLoS Genetics, Vol 11, Iss 1, p e1004903 (2015)
The mechanisms by which RNA-binding proteins control the translation of subsets of mRNAs are not yet clear. Slf1p and Sro9p are atypical-La motif containing proteins which are members of a superfamily of RNA-binding proteins conserved in eukaryotes.
Externí odkaz:
https://doaj.org/article/b192b29bdbf44b96b098f4262be44c89
Publikováno v:
BioEssays : news and reviews in molecular, cellular and developmental biologyREFERENCES. 44(11)
In recent years, membrane contact sites (MCS), which mediate interactions between virtually all subcellular organelles, have been extensively characterized and shown to be essential for intracellular communication. In this review essay, we focus on a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22315b6490cd8bafe9fdb025fdfaa83e
https://pubmed.ncbi.nlm.nih.gov/36180400
https://pubmed.ncbi.nlm.nih.gov/36180400
Publikováno v:
Frontiers in Cell and Developmental Biology. 10
Vesicle-associated membrane protein (VAMP)-associated proteins (VAPs) are ubiquitous ER-resident tail-anchored membrane proteins in eukaryotic cells. Their N-terminal major sperm protein (MSP) domain faces the cytosol and allows them to interact with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b9a77d37bf0d86f7378c7531f4aba6
https://doi.org/10.3389/fcell.2022.895856
https://doi.org/10.3389/fcell.2022.895856
Autor:
Tina A. Schrader, Ruth E. Carmichael, Markus Islinger, Joseph L. Costello, Christian Hacker, Nina A. Bonekamp, Jochen H. Weishaupt, Peter M. Andersen, Michael Schrader
Publikováno v:
Journal of cell science. 135(13)
Peroxisome membrane dynamics and division are essential to adapt the peroxisomal compartment to cellular needs. The peroxisomal membrane protein PEX11β (also known as PEX11B) and the tail-anchored adaptor proteins FIS1 (mitochondrial fission protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa7543b00958ab3df51faa98bcc60d49
https://pubmed.ncbi.nlm.nih.gov/35678336
https://pubmed.ncbi.nlm.nih.gov/35678336
Autor:
Christian Hacker, Suzan Kors, Emily J.A. Kitchener, Renate Maier, Joseph L. Costello, Michael Schrader, Bettina Warscheid, Lena Reimann, Chloe Bolton
Publikováno v:
The Journal of Cell Biology
Kors et al. reveal that peroxisome–ER associations via the ACBD5-VAPB tether are regulated by phosphorylation and GSK3β in mammalian cells. Phosphorylation sites in the FFAT-like motif of ACBD5 affect the binding to VAPB—and thus peroxisome–ER
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::063ea5c0465f36836256a6e8894057b4
https://doi.org/10.1083/jcb.202003143
https://doi.org/10.1083/jcb.202003143
Autor:
Einat Zalckvar, Stephan Kemp, Nicole Linka, Peter K. Kim, Francesca Di Cara, Joseph L. Costello, Ida J. van der Klei
Publikováno v:
Histochemistry and cell biology, 151(4), 283-289. Springer Verlag
Histochemistry and cell biology, 151(4), 283-289. SPRINGER
Histochemistry and cell biology, 151(4), 283-289. SPRINGER
The 6th Open European peroxisome meeting (OEPM) was held on the 26th and 27th of October (2018) in Groningen, the Netherlands. OEPM is a biannual meeting organized by a European peroxisome research group. Previous meetings were held in Leuven, BE (20
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::989c0228612f8b1a9217c7a7f6420224
https://doi.org/10.1007/s00418-019-01780-w
https://doi.org/10.1007/s00418-019-01780-w
Autor:
Frans A. Kuypers, Markus Islinger, Suzan Kors, Eric Soupene, Michael Schrader, Tim P. Levine, Joseph L. Costello
Publikováno v:
Biochimica et Biophysica Acta. Molecular Cell Research
Members of the large multigene family of acyl-CoA binding domain containing proteins (ACBDs) share a conserved motif required for binding of Coenzyme A esterified fatty acids of various chain length. These proteins are present in the three kingdoms o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::578dcc631d7aeb41407394b7f982fd7b
https://pubmed.ncbi.nlm.nih.gov/32044385
https://pubmed.ncbi.nlm.nih.gov/32044385
Autor:
Alexa, Bishop, Maki, Kamoshita, Josiah B, Passmore, Christian, Hacker, Tina A, Schrader, Hans R, Waterham, Joseph L, Costello, Michael, Schrader
Publikováno v:
Contact (Thousand Oaks (Ventura County, Calif.)). 2
Peroxisomes and the endoplasmic reticulum (ER) cooperate extensively in lipid-related metabolic pathways, and the ER also provides phospholipids to enable the peroxisomal membrane to expand prior to division. Recently, we identified peroxisomal prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fa8580f7459e0439519c7afaed214f27
https://pubmed.ncbi.nlm.nih.gov/31198905
https://pubmed.ncbi.nlm.nih.gov/31198905