Results 161 to 170 of about 10,800,885 (305)
Enzymatic degradation of biopolymers in amorphous and molten states: mechanisms and applications
This review explains how polymer morphology and thermal state shape enzymatic degradation pathways, comparing amorphous and molten biopolymer structures. By integrating structure–reactivity principles with insights from thermodynamics and enzyme engineering, it highlights mechanisms that enable efficient polymer breakdown.
Anđela Pustak, Aleksandra Maršavelski
wiley +1 more source
Christmas and New Year "Dietary Titbits" and Perspectives from Chronobiology. [PDF]
Erren TC, Wild U, Lewis P.
europepmc +1 more source
Chemoresistance in bladder cancer: Macrophage recruitment associated with CXCL1, CXCL5 and CXCL8 expression is characteristic of Gemcitabine/Cisplatin (Gem/Cis) Non‐Responder tumors (right side) while Responder tumors did not show substantial tumor‐stromal crosstalk (left side). All biological icons are attributed to Bioicons: carcinoma, cancerous‐cell‐
Sophie Leypold +11 more
wiley +1 more source
Looking back - Looking forward - A new year. [PDF]
Homer C.
europepmc +1 more source
BMI‐1 modulation and trafficking during M phase in diffuse intrinsic pontine glioma
The schematic illustrates BMI‐1 phosphorylation during M phase, which triggers its translocation from the nucleus to the cytoplasm. In cycling cells, BMI‐1 functions within the PRC1 complex to mediate H2A K119 monoubiquitination. Following PTC596‐induced M phase arrest, phosphorylated BMI‐1 dissociates from PRC1 and is exported to the cytoplasm via its
Banlanjo Umaru +6 more
wiley +1 more source
Promiscuous stimulation of HSP70 ATPase activity by parasite‐derived J‐domains
The malaria parasite Plasmodium falciparum exports three highly homologous yet functionally divergent J‐domain proteins into human erythrocytes. Here, we show that J‐domains isolated from all three proteins effectively stimulate the ATPase activity of both endogenous host and exported parasite HSP70 chaperones.
Julian Barth +6 more
wiley +1 more source

