Results 41 to 50 of about 3,587,930 (291)

[Intrinsically disordered proteins]. [PDF]

Postepy biochemii, 2012
Intrinsically disordered proteins (IDPs) belong to the newly discovered and still growing group of proteins. In contrast to globular proteins IDPs fail to fold into a well-defined tertiary structure under physiological conditions and they are characterized by extraordinary structural flexibility and plasticity.
Agnieszka, Dziedzic-Letka, Andrzej, Ozyhar   +1 more
  +6 more sources

Expanded Interactome of the Intrinsically Disordered Protein Dss1

Cell Reports, 2018
Summary: Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes.
Signe M. Schenstrøm, Caio A. Rebula, Michael H. Tatham, Ruth Hendus-Altenburger, Isabelle Jourdain, Ronald T. Hay, Birthe B. Kragelund, Rasmus Hartmann-Petersen   +7 more
doaj   +1 more source

Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data [PDF]

, 2009
Background: Disordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation.
Edwards, Y.J.K., Jones, DT, Pentony, MM, Jones, D.T., Edwards, YJK, Lobley, A.E., Pentony, M.M., David T Jones, Yvonne JK Edwards, Lobley, AE, Anna E Lobley, Melissa M Pentony   +11 more
core   +1 more source

Conformational Recognition of an Intrinsically Disordered Protein [PDF]

Biophysical Journal, 2014
There is a growing interest in understanding the properties of intrinsically disordered proteins (IDPs); however, the characterization of these states remains an open challenge. IDPs appear to have functional roles that diverge from those of folded proteins and revolve around their ability to act as hubs for protein-protein interactions.
Krieger J. M., Fusco G., Lewitzky M., Simister P. C., Marchant J., Camilloni C., Feller S. M., De Simone A.   +7 more
openaire   +3 more sources

Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders [PDF]

Frontiers in Aging Neuroscience, 2015
The recent years have witnessed a rise in the number of intrinsically disordered proteins (IDPs), also known as hybrid proteins, which possess both structured domains and biologically important intrinsically disordered protein regions (IDPRs). These proteins challenge the “one sequence—one structure—one function” concept by demonstrating that the lack ...
Vladimir N. Uversky, Vladimir N. Uversky, Vladimir N. Uversky, Vladimir N. Uversky   +3 more
openaire   +4 more sources

Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle [PDF]

, 2007
The potent immunomodulatory, anti-inflammatory and procoagulant properties of the protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have been previously found to be modulated by a supramolecular monomer-trimer ...
Silvia Vilasi, Raffaele Ragone, Silvia Vilasi, AND RAGONE R., VILASI, SILVIA   +4 more
core   +1 more source

Preparation of Bioderived and Biodegradable Surfactants Based on an Intrinsically Disordered Protein Sequence [PDF]

, 2021
Surfactants, block-copolymers, and other types of micellar systems are used in a wide variety of biomedical and industrial processes. However, most commonly used surfactants are synthetically derived and pose environmental and toxicological concerns ...
Matthew, Francis, Anthony, Omole, Bibiana, Onoa, Carlos, Bustamante, Sarah, Klass, Jamie, Gleason   +5 more
core   +2 more sources

Inherent structural disorder and dimerisation of murine norovirus NS1-2 protein [PDF]

, 2012
Human noroviruses are highly infectious viruses that cause the majority of acute, non-bacterial epidemic gastroenteritis cases worldwide. The first open reading frame of the norovirus RNA genome encodes for a polyprotein that is cleaved by the viral ...
Krause Kurt L., Luckner, Sylvia R., Krause, Kurt L., Luckner Sylvia R., Lambden, Paul R., Sylvia R Luckner, Kurt L Krause, Clarke, Ian N., Paul R Lambden, Baker, Estelle S., Ian N Clarke, Baker Estelle S., Estelle S Baker, Ward Vernon K., Lambden Paul R., Ward, Vernon K., Clarke Ian N., Vernon K Ward   +17 more
core   +1 more source

Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter

Frontiers in Genetics, 2018
Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are functional proteins and domains that devoid stable secondary and/or tertiary structure.
April L. Darling, Vladimir N. Uversky, Vladimir N. Uversky   +2 more
doaj   +1 more source

Theater in the Self-Cleaning Cell: Intrinsically Disordered Proteins or Protein Regions Acting with Membranes in Autophagy

Membranes, 2022
Intrinsically disordered proteins and protein regions (IDPs/IDPRs) are mainly involved in signaling pathways, where fast regulation, temporal interactions, promiscuous interactions, and assemblies of structurally diverse components including membranes ...
Hana Popelka, Vladimir N. Uversky
doaj   +1 more source