Results 51 to 60 of about 40,484 (286)

Folding factors and partners for the intrinsically disordered protein Micro-Exon Gene 14 (MEG-14)

, 2013
The micro-exon genes (MEG) of Schistosoma mansoni, a parasite responsible for the second most widely spread tropical disease, code for small secreted proteins with sequences unique to the Schistosoma genera.
Orcia, Debora, Araujo, A.P.U., Wallace, Bonnie A., Araújo, Ana Paula Ulian de, De Marco, Ricardo, Araujo, Ana Paula U., Debora Orcia, Wallace, B. A., Lopes, Jose Luiz S., DeMarco, Ricardo, Lopes, J.L.S., Ricardo DeMarco, Ana Paula U. Araujo, Orcia, D., B.A. Wallace, Wallace, B.A., Jose Luiz S. Lopes, DeMarco, R.   +17 more
core   +1 more source

A Suggestion of Converting Protein Intrinsic Disorder to Structural Entropy Using Shannon’s Information Theory

Entropy, 2019
We propose a framework to convert the protein intrinsic disorder content to structural entropy (H) using Shannon’s information theory (IT). The structural capacity (C), which is the sum of H and structural information (I), is equal to the amino acid ...
Hao-Bo Guo, Yue Ma, Gerald A. Tuskan, Hong Qin, Xiaohan Yang, Hong Guo   +5 more
doaj   +1 more source

Order, Disorder, and Everything in Between

Molecules, 2016
In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs)
Shelly DeForte, Vladimir N. Uversky
doaj   +1 more source

The N-terminal intrinsically disordered domain of mgm101p is localized to the mitochondrial nucleoid.

, 2013
The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core ...
George Desmond Clark-Walker (281878), George Desmond Clark-Walker, Dosztányi Zsuzsanna, Zsuzsanna Dosztányi (57464), Clark-Walker, George Desmond, Zsuzsanna Dosztányi, Clark-Walker George Desmond, David C. Hayward (198611), David C. Hayward, Hayward David C., Hayward, David C., Dosztányi, Zsuzsanna, David C Hayward   +12 more
core   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

FEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

Evolutionarily conserved network properties of intrinsically disordered proteins. [PDF]

PLoS ONE, 2015
Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners.
Nivedita Rangarajan, Prakash Kulkarni, Sridhar Hannenhalli   +2 more
doaj   +1 more source

Organ‐specific redox imbalances in spinal muscular atrophy mice are partially rescued by SMN antisense oligonucleotides

FEBS Letters, EarlyView.
We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley   +1 more source

Templated folding of intrinsically disordered proteins [PDF]

, 2020
Much of our current knowledge of biological chemistry is founded in the structure-function relationship, whereby sequence determines structure that determines function. Thus, the discovery that a large fraction of the proteome is intrinsically disordered,
Troilo F., Brunori M., Malagrino Francesca, Jemth P., Gianni S., Visconti L., Pagano L., Toto A.   +7 more
core   +2 more sources

Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins

Biomolecules, 2021
Motifs within proteins help us categorize their functions. Intrinsically disordered proteins (IDPs) are rich in short linear motifs, conferring them many different roles.
Estella A. Newcombe, Catarina B. Fernandes, Jeppe E. Lundsgaard, Inna Brakti, Kresten Lindorff-Larsen, Annette E. Langkilde, Karen Skriver, Birthe B. Kragelund   +7 more
doaj   +1 more source

Unequivocal single-molecule force spectroscopy of intrinsically disordered proteins [PDF]

, 2012
Intrinsically disordered proteins (IDPs) are predicted to represent about one third of the eukaryotic proteome. The dynamic ensemble of conformations of this steadily growing class of proteins has remained hardly accessible for bulk biophysical ...
Rubén Hervás, Carrión-Vázquez, Mariano Sixto, Carrión-Vázquez, Mariano, Oroz, Javier, Valbuena, Alejandro, Hervás, Rubén, Javier Oroz, Alejandro Valbuena, Mariano Carrión-Vázquez   +8 more
core   +1 more source