Results 151 to 160 of about 1,827 (179)

Selenoprotein S associates with complexes governing membrane protein biogenesis and translation-associated processes. [PDF]

open access: yesRedox Biol
Ghelichkhani F   +7 more
europepmc   +1 more source

The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria

open access: yesJournal of Cell Biology, 2009
Prohibitin ring complexes in the mitochondrial inner membrane regulate cell proliferation as well as the dynamics and function of mitochondria. Although prohibitins are essential in higher eukaryotes, prohibitin-deficient yeast cells are viable and ...
Phat Vinh Dip   +2 more
exaly   +2 more sources

Structural Requirements for the Binding of a Peptide to Prohibitins on the Cell Surface of Monocytes/Macrophages

open access: yesInternational Journal of Molecular Sciences, 2022
The screening of phage peptide libraries resulted in the identification of a sequence (named NW peptide, NWYLPWLGTNDW) that specifically binds to human monocytes and macrophages.
Mouldy Sioud, Qindong Zhang
exaly   +2 more sources

Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria

open access: yesGenes and Development, 2008
Prohibitins comprise an evolutionarily conserved and ubiquitously expressed family of membrane proteins with poorly described functions. Large assemblies of PHB1 and PHB2 subunits are localized in the inner membrane of mitochondria, but various roles in ...
Stefan Geimer   +2 more
exaly   +2 more sources
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Prohibitin and the senescent phenotype

Experimental Gerontology, 1996
Prohibitin is an evolutionarily conserved gene that has antiproliferative activity, is ubiquitously expressed, and appears to be essential for cell survival. The gene codes for a 30 kD, post-synthetically modified protein located primarily in the mitochondria.
R T, Dell'Orco   +3 more
openaire   +2 more sources

The Prohibitins: emerging roles in diverse functions [PDF]

open access: yesJournal of Cellular and Molecular Medicine, 2006
The prohibitins, Phb1 and Phb2 are highly conserved proteins in eukaryotic cells that are present in multiple cellular compartments. Initial investigations focused on the role of Phb1 as an inhibitor of cell proliferation hence the original name prohibitin.
Suresh Mishra, Leigh C Murphy
exaly   +3 more sources

Prohibitin 2: At a communications crossroads

IUBMB Life, 2015
AbstractProhibitins (PHBs) are a highly conserved class of proteins first discovered as inhibitors of cellular proliferation. Since then PHBs have been found to have a significant role in transcription, nuclear signaling, mitochondrial structural integrity, cell division, and cellular membrane metabolism, placing these proteins among the key regulators
Bavelloni A   +4 more
openaire   +2 more sources

Molecular modeling of prohibitin domains

Proteins: Structure, Function, and Bioinformatics, 2007
AbstractProhibitins comprise a family of highly conserved ubiquitous eukaryotic proteins that mainly localize to the mitochondria. They have been implicated in important cellular processes such as cellular signaling and transcriptional control, apoptosis, cellular senescence, and mitochondrial biogenesis.
Winter, Anja   +2 more
openaire   +3 more sources

Prohibitin in Adipose and Immune Functions

Trends in Endocrinology & Metabolism, 2016
Prohibitin (PHB) was discovered in a quest to find genes with antiproliferative functions. However, the attribute of PHB that is responsible for its antiproliferative function remains elusive. Meanwhile, recent studies have established PHB as a pleiotropic protein with roles in metabolism, immunity, and senescence.
Sudharsana R, Ande   +3 more
openaire   +2 more sources

Identification of prohibitin as an antigen in Behcet’s disease

Biochemical and Biophysical Research Communications, 2014
This study is intended to screen potential antigen for Behcet's disease (BD) by using human microvascular endothelial cells (HUVEC).Following cell-based indirect immunofluorescence assay with sera from BD patients, proteins extracted from HUVEC were separated and detected by Western blotting.
Yiping, Xun   +6 more
openaire   +2 more sources

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