Results 91 to 100 of about 7,902,914 (332)

A New Anatomy of Autophagic Clearance: On the Roles of Intrinsic Disorder in the Membrane-Less on Membrane-Encapsulated Mechanism

Membranes
Autophagy is a carefully regulated catabolic process that utilizes assemblies of specific sets of macromolecules operating at multiple stages of the pathway.
Vladimir N. Uversky, Hana Popelka, Daniel J. Klionsky   +2 more
doaj   +1 more source

Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation

BMC Biology, 2022
Background Current understanding of the molecular basis of memory consolidation points to an important function of amyloid formation by neuronal-specific isoforms of the cytoplasmic polyadenylation element binding (CPEB) protein family.
D. Ramírez de Mingo, D. Pantoja-Uceda, R. Hervás, M. Carrión-Vázquez, D. V. Laurents   +4 more
doaj   +1 more source

Smaller is better: nanobodies meet NMR

FEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source

Interactions by Disorder – A Matter of Context

Frontiers in Molecular Biosciences, 2020
Living organisms depend on timely and organized interactions between proteins linked in interactomes of high complexity. The recent increased precision by which protein interactions can be studied, and the enclosure of intrinsic structural disorder ...
Katrine Bugge, Katrine Bugge, Inna Brakti, Inna Brakti, Catarina B. Fernandes, Catarina B. Fernandes, Jesper E. Dreier, Jesper E. Dreier, Jeppe E. Lundsgaard, Jeppe E. Lundsgaard, Johan G. Olsen, Johan G. Olsen, Karen Skriver, Birthe B. Kragelund, Birthe B. Kragelund   +14 more
doaj   +1 more source

Protein intrinsically disordered region prediction by combining neural architecture search and multi-objective genetic algorithm

BMC Biology, 2023
Background Intrinsically disordered regions (IDRs) are widely distributed in proteins and related to many important biological functions. Accurately identifying IDRs is of great significance for protein structure and function analysis.
Yi-Jun Tang, Ke Yan, Xingyi Zhang, Ye Tian, Bin Liu   +4 more
doaj   +1 more source

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G., Hay, Ronald T., Larsen, Ida B., Kragelund, Birthe B., Tatham, Michael H, Rösner, Heike I, Kragelund, Birthe Brandt, Hay, Ronald T, Kragelund, Birthe B, Kriegenburg, Franziska, Tatham, Michael H., Rösner, Heike Ilona, Paraskevopoulos, Konstantinos, Brandstrup, Rikke, Larsen, Ida B, Medina, Bethan; id_orcid, Hartmann-Petersen, Rasmus, Gordon, Colin, Rösner, Heike I., Hardwick, Kevin G, Medina, Bethan   +20 more
core   +1 more source

Soft motions encoded by the fold and mediated by conserved hinge sites drive V‐ATPase allosteric machinery and autoinhibition

FEBS Letters, EarlyView.
Vacuolar H+‐ATPase (V‐ATPase) is a multisubunit rotary proton pump that acidifies intracellular compartments. Using elastic network models, we identified conserved hinge residues that govern its large‐scale functional motions. We show that intrinsically encoded ‘soft modes’ drive critical functional transitions, including rotary catalysis and ...
Diksha Parwana, Xiaowei Bogetti, Stuti Sharma, Ivet Bahar   +3 more
wiley   +1 more source

Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics

Frontiers in Physics, 2019
Recognition of the natural abundance and functional importance of intrinsically disordered proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions (IDPRs) and ordered regions, is changing protein science.
Vladimir N. Uversky, Vladimir N. Uversky
doaj   +1 more source

Enhancing Binding Affinity of an Intrinsically Disordered Protein by α-Methylation of Key Amino Acid Residues [PDF]

, 2019
Intrinsically disordered proteins (IDPs), which undergo folding upon binding to their targets, are critical players in protein interaction networks.
Gilles, Travé, Natacha, Rochel, Vladimir, Torbeev, Camille, Kostmann, Bruno, Kieffer, Alexandra, Cousido-Siah, Boris, Schmidtgall, Gergő, Gógl, André, Mitschler, Judit, Osz, Jozica, Dolenc, Valentin, Bauer, Yves, Nominé   +12 more
core   +1 more source

An assignment of intrinsically disordered regions of proteins based on NMR structures [PDF]

Journal of Structural Biology, 2013
Intrinsically disordered proteins (IDPs) do not adopt stable three-dimensional structures in physiological conditions, yet these proteins play crucial roles in biological phenomena. In most cases, intrinsic disorder manifests itself in segments or domains of an IDP, called intrinsically disordered regions (IDRs), but fully disordered IDPs also exist ...
Motonori, Ota, Ryotaro, Koike, Takayuki, Amemiya, Takeshi, Tenno, Pedro R, Romero, Hidekazu, Hiroaki, A Keith, Dunker, Satoshi, Fukuchi   +7 more
openaire   +2 more sources