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ProteomicsThe conserved NUS-1/DHDDS-1 complex links N-glycosylation to lipid and lysosomal homeostasis in C. elegans
Using the nematode Caenorhabditis elegans as a model animal system, this study aims to investigate and elucidate the detailed pathogenic mechanisms by which mutations in the cis-prenyltransferase (cis-PT) complex, which plays an essential role in the human N-glycosylation pathway, lead to the develo...
ORGANISM(S): Caenorhabditis elegans 
2026-09-25 | PXD084420 | Pride
C. elegans Cis-pt 
ProteomicsStructural mechanisms of allosteric regulation in the human cis-prenyltransferase complex
Human cis-prenyltransferase (hcis-PT) synthesizes long-chain isoprenoids essential for N-linked protein glycosylation. This heteromeric complex comprises the catalytic subunit DHDDS and the regulatory Nogo-B receptor (NgBR). Although NgBR dramatically enhances DHDDS activity, the molecular basis for...
ORGANISM(S): Homo sapiens (Human) 
2025-10-20 | PXD063722 | Pride
Nogo-b receptor Allosteric regulation Dehydrodolichyl diphosphate synthase Cis-prenyltransferase Dhdds N-linked glycosylation Molecular dynamics simulations Hydrogen-deuterium exchange mass spectrometry Network analysis Ngbr 
ProteomicsStructural analysis of human cis-prenyltransferase
Isoprenoids are synthesized by the prenyltransferases superfamily, which is subdivided according to the product stereoisomerism and length. In short- and medium-chain isoprenoids, product length correlates with active site volume. However, enzymes synthesizing long-chain products and rubber synthase...
ORGANISM(S): Homo sapiens (Human) 
2022-06-09 | PXD031707 | Pride
Cis-prenyltransferase H/d exchange mass spectrometry Isoprenoid synthesis 
ProteomicsStructural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.
Strcutural analysis of human cis-prenyltrasnferase showing its architecture in solution as heterotetramer composed of two catalytic dehydrodolichyl diphosphate synthase (DHDDS)units and two inactive Nogo-B receptor (NgBR) units.
ORGANISM(S): Homo sapiens (Human) 
2022-02-15 | PXD021591 | Pride
Heterotetramer N-glycosylation Native ms Human cis-pt 
UnknownStructural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.
Not available
S-EPMC7573591 | biostudies-literature
UnknownStructural mechanisms of allosteric regulation in the human cis-prenyltransferase complex.
Not available
S-EPMC12663261 | biostudies-literature
TranscriptomicsDirect androgen receptor regulation of sexually dimorphic gene expression in the mammalian kidney
Mammalian organs exhibit distinct physiology, disease susceptibility and injury responses between the sexes. In the mouse kidney, sexually dimorphic gene activity maps predominantly to proximal tubule (PT) segments. Bulk RNA-seq data analyses demonstrated sex differences were established from 4 and ...
ORGANISM(S): Mus musculus 
2023-08-02 | GSE225566 | GEO
TranscriptomicsDifferential gene expression for A2780 human ovarian cancer cells when exposed to a new osmium-based anticancer agent
Platinum-based metallodrugs are the most widely used anticancer agents. Their reduced effectiveness after repeat dosing (resistance) constitutes a major clinical problem. In this experiment we study a potent organo-osmium compound with improved activity over cisplatin and no cross-resistance in plat...
ORGANISM(S): Homo sapiens 
2016-05-22 | E-MTAB-2758 | biostudies-arrayexpress
UnknownPentoxifylline Sensitizes Cisplatin-Resistant Human Cervical Cancer Cells to Cisplatin Treatment: Involvement of Mitochondrial and NF-Kappa B Pathways.
Not available
S-EPMC7931705 | biostudies-literature
UnknownInvestigations of the Kinetics and Mechanism of Reduction of a Carboplatin Pt(IV) Prodrug by the Major Small-Molecule Reductants in Human Plasma.
Not available
S-EPMC6888404 | biostudies-literature
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