Results 221 to 230 of about 29,414 (258)

A Disorder-Aware Computational Framework to Identify Structurally Tractable Targets in Proliferative Vitreoretinopathy. [PDF]

Ophthalmol Sci
Djulbegovic MB, Hadzijahic N, Taylor Gonzalez DJ, Antonietti M, Zafar S, Kuriyan AE.   +5 more
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Protein-protein interaction inhibitors in the human proteome: lessons from 117 targeted interactions. [PDF]

RSC Med Chem
Hyde EE, Beekman AM.
europepmc   +1 more source

Structure and molecular function of the BCL7 proteins. [PDF]

Biochem Soc Trans
Martin F, Bergamin E.
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Accurate interdomain contacts in a mixed folded protein from NMR-guided coarse-grained simulations.

Phys Chem Chem Phys
Hobbs B, Limmer N, Clenshaw GL, Ossa F, Karamanos TK.   +4 more
europepmc   +1 more source

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Intrinsically disordered protein regions at membrane contact sites

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2021
Membrane contact sites (MCS) are regions of close apposition between membrane-bound organelles. Proteins that occupy MCS display various domain organisation. Among them, lipid transfer proteins (LTPs) frequently contain both structured domains as well as regions of intrinsic disorder.
Denisa, Jamecna, Bruno, Antonny
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Intrinsically disordered proteins/regions and insight into their biomolecular interactions

Biophysical Chemistry, 2022
Proteins may vary from being rigid to having flexible regions to being completely disordered, either as an intrinsically disordered protein (IDP) or having specific intrinsically disordered regions (IDRs). IDPs/IDRs can form complexes otherwise impossible, such as wrapping around the binding partner, hence providing the plasticity needed for achieving ...
Pinak, Chakrabarti, Devlina, Chakravarty
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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Annual Review of Biochemistry, 2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
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Prediction of the Disordered Regions of Intrinsically Disordered Proteins Based on the Molecular Functions

Protein & Peptide Letters, 2020
Background: Intrinsically disordered proteins lack a well-defined three dimensional structure under physiological conditions while possessing the essential biological functions. They take part in various physiological processes such as signal transduction, transcription and posttranslational modifications and etc.
WeiXia, Xie, Yong E, Feng
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