Results 51 to 60 of about 23,171 (195)
Nature Communications, 2023 Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes and hold promise as drug targets. However, the dynamic nature of IDPs remains poorly understood.
Wenzhe Liu +7 more
semanticscholar +1 more source
Actinidia DRM1--an intrinsically disordered protein whose mRNA expression is inversely correlated with spring budbreak in kiwifruit. [PDF]
PLoS ONE, 2013 Intrinsically disordered proteins (IDPs) are a relatively recently defined class of proteins which, under native conditions, lack a unique tertiary structure whilst maintaining essential biological functions.
Marion Wood +6 more
doaj +1 more source
Dynamics and interactions of intrinsically disordered proteins.
Current Opinion in Structural Biology, 2023 Intrinsically disordered proteins (IDPs) are widespread in eukaryotes and participate in a variety of important cellular processes. Numerous studies using state-of-the-art experimental and theoretical methods have advanced our understanding of IDPs and ...
M. Arai, Shunji Suetaka, Koji Ooka
semanticscholar +1 more source
An Evolutionary Algorithm for the Design of Different Degrees of Secondary Structure in Intrinsically Disordered Proteins (IDPs) [PDF]
Biophysical Journal, 2015 In recent experimental studies of coupled folding and binding of IDPs investigators have adapted methods from the protein folding literature whereby point mutations are used to identify the degree to which different regions are pre-folded prior to the rate limiting step in binding and folding. These approaches assume a one-to-one correspondence between
Harmon, Tyler S., Pappu, Rohit V.
openaire +1 more source
Molecular & Cellular Oncology, 2019 Intrinsically disordered proteins (IDPs) do not have a well-defined structure, but they have key biological tasks in cancer development. By using the disordered cancer-related protein NUPR1 as a proof-of-concept, we have developed a new multidisciplinary
Patricia Santofimia-Castaño +7 more
doaj +1 more source
Diffusing protein binders to intrinsically disordered proteins
NatureProteins that bind to intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) with high affinity and specificity could be useful for therapeutic and diagnostic applications1, 2, 3–4.
Caixuan Liu +31 more
semanticscholar +2 more sources
Conformational entropy in molecular recognition of intrinsically disordered proteins.
Current Opinion in Structural Biology, 2023 Broad conformational ensembles make intrinsically disordered proteins or regions entropically intriguing. Although methodologically challenging and understudied, emerging studies into their changes in conformational entropy (ΔS°conf) upon complex ...
K. Skriver, F. Theisen, B. Kragelund
semanticscholar +1 more source
Angewandte Chemie, EarlyView.Oncogenic MYC is a transcription factor that is difficult to inhibit. However, precise positioning of an acrylamide electrophile in MAX to covalently bond to the unique Cys438 in MYC, enabled shortening and optimizing of MAX‐derived, helix‐constrained peptides with high‐affinity and selectivity.
Aline Dantas de Araujo +7 more
wiley +2 more sources
Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins
Biomolecules, 2020 Direct interaction between intrinsically disordered proteins (IDPs) is often difficult to characterize hampering the elucidation of their binding mechanism.
Maria Grazia Murrali +2 more
doaj +1 more source
Deciphering Mode of Action of Functionally Important Regions in the Intrinsically Disordered Paxillin (Residues 1-313) Using Its Interaction with FAT (Focal Adhesion Targeting Domain of Focal Adhesion Kinase). [PDF]
PLoS ONE, 2016 Intrinsically disordered proteins (IDPs) play a major role in various cellular functions ranging from transcription to cell migration. Mutations/modifications in such IDPs are shown to be associated with various diseases.
Muniasamy Neerathilingam +2 more
doaj +1 more source