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Published in 2022 at "Biophysical journal"
DOI: 10.1016/j.bpj.2022.04.017
Abstract: Biological functions of proteins rely on their specific interactions with binding partners. Many proteins contain multiple domains, which can bind to their targets that often have more than one binding site, resulting in multivalent interactions.…
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Keywords:
domain;
binding affinity;
multivalent interactions;
affinity specificity ... See more keywords
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Published in 2018 at "Structure"
DOI: 10.1016/j.str.2017.11.003
Abstract: Many regulatory proteins, including the transcription factor c-Jun, are highly enriched in disordered protein regions that govern growth, division, survival, differentiation, and response to signals. The stability of c-Jun is controlled by poorly understood regulatory…
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Keywords:
jun;
ubiquitin ligase;
interactions fbw7;
multivalent interactions ... See more keywords
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Published in 2019 at "Polymer Journal"
DOI: 10.1038/s41428-018-0168-x
Abstract: Dendrimers, a type of dendritic molecule, have a well-defined structure with a homogeneous molecular weight and precise multiple terminal groups. These characteristics are favorable for both research and development, which require accuracy and multivalency. This…
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Keywords:
biological functionality;
biological recognition;
loosely packed;
packed terminals ... See more keywords
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Published in 2022 at "Essays in Biochemistry"
DOI: 10.1042/ebc20220056
Abstract: Abstract The spatial and temporal organization of interactions between proteins underlie the regulation of most cellular processes. The requirement for such interactions to be specific predisposes a view that protein–protein interactions are relatively static and…
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Keywords:
nmr insights;
interactions intrinsically;
intrinsically disordered;
multivalent interactions ... See more keywords