Results 51 to 60 of about 559,331 (298)

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

open access: yesFEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li   +2 more
wiley   +1 more source

High mobility group box-1: a potential therapeutic target for allergic rhinitis

open access: yesEuropean Journal of Medical Research, 2023
Allergic rhinitis (AR) is a prevalent chronic inflammatory disease of the nasal mucosa primarily characterized by symptoms, such as nasal itching, sneezing, runny nose, and nasal congestion. It has a high recurrence rate and low cure rate, with a lack of
Shuhua Wu   +3 more
doaj   +1 more source

Many faces of DAMPs in cancer therapy [PDF]

open access: yes, 2013
A new concept of immunogenic cell death (ICD) has recently been proposed. The immunogenic characteristics of this cell death mode are mediated mainly by molecules called ‘damage-associated molecular patterns’ (DAMPs), most of which are recognized by ...
Aaes, Tania Love   +4 more
core   +1 more source

High-Mobility Group Box-1 in Ischemia-Reperfusion Injury of the Heart [PDF]

open access: yesCirculation, 2008
Background— High-mobility group box-1 (HMGB1) is a nuclear factor released by necrotic cells and by activated immune cells. HMGB1 signals via members of the toll-like receptor family and the receptor for advanced glycation end products (RAGE).
Andrassy, Martin   +18 more
openaire   +2 more sources

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

open access: yesFEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa   +5 more
wiley   +1 more source

Sample Preparation Strategies for Antibody-Free Quantitative Analysis of High Mobility Group Box 1 Protein

open access: yesPharmaceuticals, 2021
Sickness behavior and fatigue are induced by cerebral mechanisms involving inflammatory cytokines. High mobility group box 1 (HMGB1) is an alarmin, and a potential key player in this process.
Ingeborg Kvivik   +3 more
doaj   +1 more source

Cutting edge: extracellular high mobility group box-1 protein is a proangiogenic cytokine. [PDF]

open access: yes, 2006
The chromosomal high mobility group box-1 (HMGB1) protein acts as a proinflammatory cytokine when released in the extracellular environment by necrotic and inflammatory cells.
BELLERI M   +7 more
core  

Early release of high mobility group box nuclear protein 1 after severe trauma in humans: role of injury severity and tissue hypoperfusion [PDF]

open access: yes, 2009
IntroductionHigh mobility group box nuclear protein 1 (HMGB1) is a DNA nuclear binding protein that has recently been shown to be an early trigger of sterile inflammation in animal models of trauma-hemorrhage via the activation of the Toll-like-receptor ...
Mitchell J Cohen   +8 more
core   +2 more sources

High-Mobility Group Box 1 in Dry Eye Inflammation

open access: yesInvestigative Opthalmology & Visual Science, 2018
To determine high-mobility group box 1 (HMGB1) expression during experimental dry eye (EDE) and dry eye-like culture conditions and elucidate its role in corneal dry eye-related inflammation.EDE was induced in 8- to 12-week-old C57BL/6 mice. Corneal tissue sections and lysates from EDE and untreated mice were evaluated for HMGB1 expression by ...
Lema, Carolina   +2 more
openaire   +2 more sources

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

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