Results 101 to 110 of about 7,902,914 (332)

Unlocking the potential of cell‐permeable nanobodies for intracellular applications

FEBS Letters, EarlyView.
This review outlines current strategies for delivery of nanobodies into cells and highlights recent examples of functional applications. By addressing and manipulating intracellular targets, these molecules hold great potential for treating cancer, respiratory diseases and neurological disorders, making this a vibrant area of research in the biomedical
Mariona Gené‐Verdés, Luise Franz, Christian P.R. Hackenberger   +2 more
wiley   +1 more source

Proteasomal degradation of the intrinsically disordered protein tau at single-residue resolution

Science Advances, 2020
Dissecting the degradation of the Alzheimer’s disease–related protein Tau by the 20S proteasome at single-residue resolution. Intrinsically disordered proteins (IDPs) can be degraded in a ubiquitin-independent process by the 20S proteasome.
T. Ukmar-Godec, P. Fang, A. I. de Opakua, F. Henneberg, A. Godec, K. Pan, Maria-Sol Cima-Omori, A. Chari, E. Mandelkow, H. Urlaub, M. Zweckstetter   +10 more
semanticscholar   +1 more source

Exon-phase symmetry and intrinsic structural disorder promote modular evolution in the human genome [PDF]

, 2013
A key signature of module exchange in the genome is phase symmetry of exons, suggestive of exon shuffling events that occurred without disrupting translation reading frame.
Kalmár, Lajos, Schád, Éva, Tompa, Péter   +2 more
core   +1 more source

Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins [PDF]

Biomolecules, 2019
One of the unique characteristics of intrinsically disordered proteins (IPDs) is the existence of functional segments in intrinsically disordered regions (IDRs). A typical function of these segments is binding to partner molecules, such as proteins and DNAs. These segments play important roles in signaling pathways and transcriptional regulation.
Anbo, Hiroto, Sato, Masaya, Okoshi, Atsushi, Fukuchi, Satoshi   +3 more
openaire   +3 more sources

CARs-DB: A Database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins

Frontiers in Molecular Biosciences, 2022
Proteome-wide analyses suggest that most globular proteins contain at least one amyloidogenic region, whereas these aggregation-prone segments are thought to be underrepresented in intrinsically disordered proteins (IDPs). In recent work, we reported that intrinsically disordered regions (IDRs) indeed sustain a significant amyloid load in the form of ...
Pintado-Grima, Carlos, Bárcenas, Oriol, Manglano-Artuñedo, Zoe, Vilaça, Rita, Macedo-Ribeiro, Sandra, Pallarès, Irantzu, Santos, Jaime, Ventura, Salvador   +7 more
openaire   +4 more sources

How structural disorder and polyelectrolyte properties of prothymosin α enable its large interactome

FEBS Letters, EarlyView.
In this review, complexes of the fully disordered and highly negatively charged prothymosin α are collected, described, and discussed. Linked to its poly‐electrostatic character, prothymosin α engages a large interactome through multiple different binding modes ranging from fully disordered complexes to short linear motif (SLiM)‐driven interactions ...
Ketty C. Tamburrini, Freia S. Buus, Benjamin Schuler, Birthe B. Kragelund   +3 more
wiley   +1 more source

A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR [PDF]

International Journal of Molecular Sciences, 2015
Intrinsically disordered proteins (IDPs) that lack stable conformations and are highly flexible have attracted the attention of biologists. Therefore, the development of a systematic method to identify polypeptide regions that are unstructured in solution is important.
Natsuko Goda, Kana Shimizu, Yohta Kuwahara, Takeshi Tenno, Tamotsu Noguchi, Takahisa Ikegami, Motonori Ota, Hidekazu Hiroaki   +7 more
openaire   +2 more sources

The ‘Shape-Shifter’ Peptide from the Disulphide Isomerase PmScsC Shows Context-Dependent Conformational Preferences

Biomolecules, 2021
Multiple crystal structures of the homo-trimeric protein disulphide isomerase PmScsC reveal that the peptide which links the trimerization stalk and catalytic domain can adopt helical, β-strand and loop conformations. This region has been called a ‘shape-
Lorna J. Smith, Chloe W. Green, Christina Redfield   +2 more
doaj   +1 more source

Mitochondrial translation and coordinated cytosolic translation in metabolic homeostasis and disease

FEBS Letters, EarlyView.
Mitochondrial function depends on coordinated protein production from the nuclear and mitochondrial genomes. This review highlights how cytosolic and mitochondrial translation, mRNA localization, protein import, and respiratory complex assembly are integrated to maintain mitochondrial proteostasis and function.
Boseon Kim, Thi Thanh Mai Tran, Nakyung Kang, Min‐Woo Lee, Mihye Lee   +4 more
wiley   +1 more source

A blurry view of fuzzy objects: on the roles of low-resolution structural techniques in discovery and early characterization of intrinsically disordered proteins

Frontiers in Biophysics
The discovery of intrinsically disordered proteins (IDPs) (and, therefore, the establishment of the field of protein intrinsic disorder) was initially driven by low-resolution techniques, which overturned the established “lock-and-key” paradigm of ...
Vladimir N. Uversky
doaj   +1 more source