Results 231 to 240 of about 30,178 (280)
Harnessing Cuproptosis for Antitumor Immunity: A Review of Current Evidence and Therapeutic Strategies. [PDF]
Lu I, Zhang J, Chen X, Wang XJ.
europepmc +1 more source
The Dual Mechanism of Action of CO-005 Overcomes CD20 Resistance in Diffuse Large B-Cell Lymphoma. [PDF]
Matar S +7 more
europepmc +1 more source
Calreticulin in the nasal mucus promotes neutrophil migration and pathogen clearance. [PDF]
Ma Y +6 more
europepmc +1 more source
Boosting immunogenic tumour cell death via nanotherapeutic targeting of the Stanniocalcin 1 phagocytosis checkpoint for enhanced cancer immunotherapy. [PDF]
Li W +7 more
europepmc +1 more source
Conformational Stability of Calreticulin
The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31 degrees C at pH 5 to 51 degrees C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding.
Jørgensen, Charlotte S +8 more
core +5 more sources
Chemical and Thermal Unfolding of Calreticulin
Calreticulin is a soluble endoplasmic reticulum chaperone, which has a relatively low melting point due to its remarkable structure with a relatively high content of flexible structural elements. Using far ultraviolet circular dichroism (CD) spectroscopy and a fluorescent dye binding thermal shift assay, we have investigated the chemical and thermal ...
Duus, K. +7 more
core +4 more sources
Calreticulin, a therapeutic target? [PDF]
Introduction: Calreticulin is an endoplasmic reticulum (ER) resident protein critical for maintaining Ca2+ homeostasis and glycoprotein folding in the ER.
Paul Eggleton +2 more
exaly +2 more sources
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The International Journal of Biochemistry & Cell Biology, 1998
Calreticulin is an ancient and highly conserved protein. It is intensively studied and has been assigned multiple functions, the scope and variety of which are exceptionally wide for a single protein. Subsequent to the description of its calcium binding properties, calreticulin has been characterized as a molecular chaperone, an extracellular lectin ...
M G, Coppolino, S, Dedhar
openaire +2 more sources
Calreticulin is an ancient and highly conserved protein. It is intensively studied and has been assigned multiple functions, the scope and variety of which are exceptionally wide for a single protein. Subsequent to the description of its calcium binding properties, calreticulin has been characterized as a molecular chaperone, an extracellular lectin ...
M G, Coppolino, S, Dedhar
openaire +2 more sources

