Results 71 to 80 of about 29,703 (304)

Method of protein stabilization based on prediction of intrinsically disordered regions. Stabilization of protein Gαo [PDF]

, 2016
Protein Gαo from Drosophila melanogaster has been studied. We have designed an SS-bridge in this protein in such a way that its stability could be increased. The choice of a region in the polypeptide chain for insertion of the cysteine bridge was based
Melnik, Tatiana N., Melnik, Bogdan S., Glukhov, Anatoly S., Dzhus, Uliana F., Nagibina, Galina S.   +4 more
core   +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

From mice to humans—divergent strategies for intestinal homeostasis and regeneration

FEBS Letters, EarlyView.
Recent advances such as organoid genome editing, xenotransplantation, imaging, and whole‐genome sequencing have enabled direct studies of human intestinal stem cells (ISCs). These studies reveal species‐specific features, including slower ISC proliferation, distinct injury responses, slower somatic mutation accumulation in humans, and an inverse ...
Keiko Ishikawa, Shinya Sugimoto, Toshiro Sato   +2 more
wiley   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway

, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
Mainak Guharoy, Rita Pancsa (173029), Pallab Bhowmick, Tompa, Péter, Pallab Bhowmick (416342), Peter Tompa, Bhowmick, Pallab, Pancsa Rita, Guharoy Mainak, Bhowmick Pallab, Tompa Peter, Guharoy, Majnak, Mainak Guharoy (416343), Peter Tompa (38445), Rita Pancsa, Pancsa, Rita   +15 more
core   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq

, 2011
The hexameric Escherichia coli RNA chaperone Hfq (Hfq(Ec)) is involved in riboregulation of target mRNAs by small trans-encoded RNAs. Hfq proteins of different bacteria comprise an evolutionarily conserved core, whereas the C-terminus is variable in ...
Beich-Frandsen, Mads (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Kontaxis, Georg (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Blasi, U., Rajkowitsch, L., Miles, Andrew (Birkbeck College), Sjöblom, Björn (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Miles, Andrew J., Svergun, D.I., Kloiber, K., Kristina Djinović-Carugo, Vecerek, B., Karin Kloiber, Konarev, P.V., Lukas Rajkowitsch, Hämmerle, Hermann Konrad (Department of Biochemistry and Cell Biology, Centre for Molecular Biology, University of Vienna), Georg Kontaxis, Bläsi, Udo (Department of Microbiology, Immunobiology and Genetics, Centre for Molecular Biology, University of Vienna), Djinovic-Carugo, K., Robert Konrat, Branislav Večerek, Konarev, Peter V. (EMBL Hamburg), Andrew J. Miles, Kloiber, Karin (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Rajkowitsch, Lukas (Department of Biochemistry and Cell Biology, Centre for Molecular Biology, University of Vienna), Udo Bläsi, Wallace, Bonnie A., Svergun, D. I., Petr V. Konarev, Svergun, Dimitri I. (EMBL Hamburg), Björn Sjöblom, Hammerle, H., Mads Beich-Frandsen, Wallace, B. A., Sjoblom, B., Miles, A. J., Konrat, Robert (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Vecerek, Branislav (Department of Microbiology, Immunobiology and Genetics, Centre for Molecular Biology, University of Vienna), Dimitri I. Svergun, B. A. Wallace, Beich Frandsen, M., Djinovic Carugo, K., Konarev, P. V., Beich-Frandsen, M., Konrat, R., Djinovic-Carugo, Kristina (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Hermann Hämmerle, Kontaxis, G.   +46 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

Prediction of protein–protein interactions using sequences of intrinsically disordered regions

Proteins: Structure, Function, and Bioinformatics, 2023
Abstract Protein–protein interactions (PPIs) play a crucial role in numerous molecular processes. Despite many efforts, mechanisms governing molecular recognition between interacting proteins remain poorly understood and it is particularly challenging to predict from sequence whether two proteins can interact.
Gözde, Kibar, Martin, Vingron
openaire   +2 more sources

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