Results 81 to 90 of about 1,883,575 (282)

Metastatic niche shaped by host factors influences disseminated cancer cell fate

FEBS Letters, EarlyView.
Metastasis is shaped not only by cancer cells but also by the environments they encounter. This review explores how factors such as aging, diet, the microbiome, lifestyle, and environmental exposures remodel organ‐specific niches in the lung, liver, bone, and brain, influencing where metastatic cells survive, remain dormant, or grow, and ultimately ...
Gwennan Delyth Ward, Álvaro Ruiz‐Tabas, Patricia Altea‐Manzano   +2 more
wiley   +1 more source

D2P2: database of disordered protein predictions [PDF]

, 2013
We present the Database of Disordered Protein Prediction (D2P2), available at http://d2p2.pro (including website source code). A battery of disorder predictors and their variants, VL-XT, VSL2b, PrDOS, PV2, Espritz and IUPred, were run on all protein ...
Oates, Matt E., Ishida, Takashi, Dosztányi, Zsuzsanna, Romero, Pedro   +3 more
core   +1 more source

Intrinsically disordered proteins: controlled chaos or random walk

International Journal of Plant Biology, 2016
Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins.
T.C. Howton, Yingqian Ada Zhan, Yali Sun, M. Shahid Mukhtar   +3 more
doaj   +1 more source

Intrinsically disordered proteins play diverse roles in cell signaling

Cell Communication and Signaling, 2022
Signaling pathways allow cells to detect and respond to a wide variety of chemical (e.g. Ca2+ or chemokine proteins) and physical stimuli (e.g., sheer stress, light).
Sarah E. Bondos, A. Keith Dunker, Vladimir N. Uversky   +2 more
doaj   +1 more source

Data–driven Modelling of Intrinsically Disordered Proteins [PDF]

, 2019
In this thesis we investigated the relationships between amino acid sequence and biophysical properties of intrinsically disordered proteins involved in Parkinson's and Alzheimer's disease (IDPs), gauged from NMR ...
Tamiola, Kamil
core   +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

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

, 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 ...
Blasi, U., Rajkowitsch, L., Miles, Andrew J., Svergun, D.I., Kloiber, K., Kristina Djinović-Carugo, Vecerek, B., Karin Kloiber, Konarev, P.V., Lukas Rajkowitsch, Georg Kontaxis, Djinovic-Carugo, K., Robert Konrat, Branislav Večerek, Andrew J. Miles, Udo Bläsi, Wallace, Bonnie A., Svergun, D. I., Petr V. Konarev, Björn Sjöblom, Hammerle, H., Mads Beich-Frandsen, Wallace, B. A., Sjoblom, B., Miles, A. J., Dimitri I. Svergun, B. A. Wallace, Beich Frandsen, M., Djinovic Carugo, K., Konarev, P. V., Beich-Frandsen, M., Konrat, R., Hermann Hämmerle, Kontaxis, G.   +33 more
core   +1 more source

Invisible but not inaccessible—Revealing transient oligomers formed by intrinsically disordered proteins with solution NMR and complementary methods

FEBS Letters, EarlyView.
Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley   +1 more source

Protein order and disorder: A quantitative in silico analysis [PDF]

EPJ Web of Conferences
Proteins are fundamental biological macromolecules responsible for a wide range of cellular functions. Traditionally, a central paradigm linked the amino acid sequence to a unique, ordered three-dimensional structure that underlies biological activity ...
de Brevern Alexandre G.
doaj   +1 more source

SCREENING INTERACTIONS BETWEEN PROTEINS AND DISORDERED PEPTIDES BY A NOVEL COMPUTATIONAL METHOD [PDF]

, 2013
Concerted interactions between proteins in cells form the basis of most biological processes. Biophysicists study protein–protein association by measuring thermodynamic and kinetic properties.
Zhang, Weiyi
core