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The prodrug strategy used in this study offers new promise for cancer metabolism‐based therapies. JHU083, a prodrug that, when cleaved by protease in the tumor microenvironment, yields the glutamine antagonist DON. JHU083 inhibits tumor growth by targeting glutamine‐addicted cancer cells and suppressing glutamine‐dependent M2 macrophages, leading to a ...
Tianhe Li+10 more
wiley +1 more source
Unlocking the power of AI models: exploring protein folding prediction through comparative analysis. [PDF]
Tejera-Nevado P+4 more
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HMGB1 derived from the pyroptotic environment in Hirschsprung‐associated enterocolitis mediates the formation of macrophage extracellular traps through TLR4 ‐p38 MAPK/p65 NF‐kB signaling pathways. Macrophage extracellular traps induce increased ROS production and pyroptosis of colonic epithelial cells.
Rui Zhang+6 more
wiley +1 more source
Most Monogenic Disorders Are Caused by Mutations Altering Protein Folding Free Energy. [PDF]
Pandey P, Alexov E.
europepmc +1 more source
Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification. [PDF]
Scaletti C+8 more
europepmc +1 more source
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Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape
Angewandte Chemie - International Edition, 2018Protein folding involves a large number of steps and conformations in which the folding protein samples different thermodynamic states characterized by local minima.
Jozef Adamcik+2 more
exaly +2 more sources
Protein folding in the cell [PDF]
M. Gething, J. Sambrook
semanticscholar +3 more sources
Quarterly Reviews of Biophysics, 1977
This review describes recent advances in studies on the stabilities of the three-dimensional structures of proteins and on the processes leading to the formation of these structures. The term ‘protein folding’ will be used here to denote the process of the conversion of an open polypeptide chain into the unique three-dimensional conformation of the ...
G, Némethy, H A, Scheraga
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This review describes recent advances in studies on the stabilities of the three-dimensional structures of proteins and on the processes leading to the formation of these structures. The term ‘protein folding’ will be used here to denote the process of the conversion of an open polypeptide chain into the unique three-dimensional conformation of the ...
G, Némethy, H A, Scheraga
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Dominant forces in protein folding.
Biochemistry, 1990T e purpose of this review is to assess the nature and magnitudes of the dominant forces in protein folding. Since proteins are only marginally stable at room temperature,’ no type of molecular interaction is unimportant, and even small interactions can ...
K. Dill
semanticscholar +1 more source
Annual Review of Biochemistry, 1981
After some general remarks on protein structure, there follows a discussion on primary, secondary, and tertiary organization. The account of primary structure includes a discussion of the conformation of disulfide bonds. Types of helices, sheets, and turns are described in the section on secondary structure, followed by a discussion of super-secondary ...
M G, Rossmann, P, Argos
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After some general remarks on protein structure, there follows a discussion on primary, secondary, and tertiary organization. The account of primary structure includes a discussion of the conformation of disulfide bonds. Types of helices, sheets, and turns are described in the section on secondary structure, followed by a discussion of super-secondary ...
M G, Rossmann, P, Argos
openaire +2 more sources