Results 71 to 80 of about 7,315 (215)

Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones. [PDF]

open access: yesPLoS Pathogens, 2009
The physiological environment which hosts the conformational conversion of the cellular prion protein (PrP(C)) to disease-associated isoforms has remained enigmatic.
Joel C Watts   +13 more
doaj   +1 more source

Proteome Analysis of Corynebacterium diphtheriae–Macrophage Interaction

open access: yesPROTEOMICS, EarlyView.
ABSTRACT Contact of Corynebacterium diphtheriae with macrophages induces adaptations on both bacterial and cellular sides. The study presented here was aiming to shed light on the simultaneous intracellular adaptation of the bacteria and changes in the proteome of the phagocytes in response to the internalization of C. diphtheriae.
Luca Musella   +6 more
wiley   +1 more source

AGR2-mediated cell-cell communication controls the antiviral immune response by promoting the thiol oxidation of TRAF3

open access: yesRedox Biology
Protein disulfide isomerases (PDIs) are essential catalysts for the formation and isomerization of disulfide bonds in diverse substrate proteins and exert multiple functions under pathophysiological conditions.
Mengqi Jia   +13 more
doaj   +1 more source

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor. [PDF]

open access: yes, 2006
The nematode Caenorhabditis elegans represents an excellent model in which to examine nematode gene expression and function. A completed genome, straightforward transgenesis, available mutants and practical genome-wide RNAi approaches provide an ...
Andrew J. Birnie   +42 more
core   +1 more source

Comparative Analysis of Heat Exposure‐Induced Molecular Changes in Two Turtle Species with Contrasting Thermal Adaptations

open access: yesIntegrative Zoology, EarlyView.
Protein processing in the endoplasmic reticulum is highlighted in response to heat stress in Platysternon megacephalum. Under heat stress, the up‐regulation of genes such as CHOP in protein processing in the endoplasmic reticulum pathway, along with the suppression of energy and lipid metabolism and the up‐regulation of JARID2 expression, leads to ...
Jian Hong   +7 more
wiley   +1 more source

Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection

open access: yesRetrovirology, 2012
Background The role of disulfide bond remodeling in HIV-1 infection is well described, but the process still remains incompletely characterized. At present, the data have been predominantly obtained using established cell lines and/or CXCR4-tropic ...
Stantchev Tzanko S   +5 more
doaj   +1 more source

Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion. [PDF]

open access: yes, 2017
Blood banks use pathogen inactivation (PI) technologies to increase the safety of platelet concentrates (PCs). The characteristics of PI-treated PCs slightly differ from those of untreated PCs, but the underlying reasons are not well understood.
Abonnenc, M.   +4 more
core   +1 more source

Targeting protein–protein interactions with reversible covalent modalities: Non‐cysteine chemistries

open access: yesBritish Journal of Pharmacology, EarlyView.
Abstract Protein–protein interactions (PPIs) are central to diverse cellular functions, and represent a rapidly expanding class of therapeutic targets. Advancements in covalent drug design have enabled small‐molecule drugs to overcome challenges associated with engaging these targets, such as limited durations of action and difficult‐to‐drug (expansive,
Ruchira Basu, Steven Fletcher
wiley   +1 more source

The Crucial Role of Demannosylating Asparagine-Linked Glycans in ERADicating Misfolded Glycoproteins in the Endoplasmic Reticulum

open access: yesFrontiers in Plant Science, 2021
Most membrane and secreted proteins are glycosylated on certain asparagine (N) residues in the endoplasmic reticulum (ER), which is crucial for their correct folding and function.
Jianjun Zhang   +8 more
doaj   +1 more source

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor [PDF]

open access: yes, 2013
ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known.
Braakman, Ineke   +4 more
core   +1 more source

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