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ProteomicsTTYH family members form tetrameric complexes at the cell membrane
The conserved Tweety homolog (TTYH) family consists of three paralogs in vertebrates, displaying a ubiquitous expression pattern. Although considered as ion channels for almost two decades, recent structural and functional analyses refuted this role. Intriguingly, while all paralogs shared a dimeric...
ORGANISM(S): Mus musculus (Mouse) 
2022-08-31 | PXD031833 | Pride
Tweety homolog family Ttyh Dimer Tetramer Hydrogen/deuterium exchange 
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 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 
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 
ProteomicsHsp70 ATP-dependent dimerization and Chaperone/Co-chaperone Interactions
Eukaryotic protein homeostasis (proteostasis) is largely dependent on the action of highly conserved Hsp70 molecular chaperones. Recent evidence indicates that apart from conserved molecular allostery, Hsp70 proteins retained and adapted throughout the evolution the ability to assemble as functional...
ORGANISM(S): Homo sapiens (Human) 
2018-12-11 | PXD010069 | Pride
Tomm34 Hsp70 Co-chaperone Dimer Chip 
TranscriptomicsNASH
Non-alcoholic fatty liver disease (NAFLD) is characterized by a series of pathological changes that can progress from simple fatty liver disease to non-alcoholic steatohepatitis (NASH). The objective of this study is to describe changes in global gene expression associated with the progression of NA...
ORGANISM(S): Homo sapiens 
2011-07-12 | E-MEXP-3291 | biostudies-arrayexpress
TranscriptomicsMethylation profiling of different stages of human mammary epithelial cells from pre-statis to cancer
To characterize early epigenetic events in breast carcinogenesis, we analyzed DNA methylation state of different stages of HMECs from pre-stasis to cancer cell lines using human promoter microarray
ORGANISM(S): Homo sapiens 
2009-01-01 | E-MEXP-1889 | biostudies-arrayexpress
ProteomicsStructural perturbation at the N-terminal domain of human phosphoglycerate kinase 1 reduces the kinetic stability and unfolding cooperativity of a two-domain enzyme
Phosphoglycerate kinase has been a model for the stability, folding cooperativity and catalysis of a two-domain protein. The human isoform 1 (hPGK1) is associated with cancer development and rare genetic diseases that affect several of their features. To investigate how mutations affect hPGK1 foldin...
ORGANISM(S): Homo sapiens (Human) 
2022-11-03 | PXD035628 | Pride
Protein folding  structural perturbation  disease 
ProteomicsNovel calcium-binding sites in the acylated segment control the folding and membrane penetration of RTX toxins
The Repeats in ToXin (RTX) domain of RTX cytolysins harbors numerous hexacoordinated Ca2+-binding sites that facilitate cooperative and vectorial folding of the RTX β-rolls. Recent study identified Ca2+-binding sites in the acylated N-terminal extension of the RTX domain of Bordetella pertussis aden...
ORGANISM(S): Bordetella pertussis 
2026-04-22 | PXD058094 | Pride
Membrane penetration H/d exchange Rtx toxin Folding Calcium binding site Acylated segment 
ProteomicsPhenotypic divergence due to site-specific phosphorylation in the antioxidant and cancer-associated NQO1 enzyme
Aims: to evaluate the effects of site-specific phosphorylation (using phosphomimetic mutations at sites S40, S82 and T128) on multiple functional aspects of the antioxidant and disease-associated human flavoprotein NQO1. Results: in vitro biophysical studies revealed effects of phosphorylation at di...
ORGANISM(S): Homo sapiens (Human) 
2022-09-20 | PXD034600 | Pride
Flavoprotein  phosphorylation  phenotypic effects  structure-function relationships  structural stability 
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