Results 131 to 140 of about 959,641 (315)

Nuclear structure and function [PDF]

Journal of Cellular Biochemistry, 1996
Stein, Gary S., Berezney, Ronald
openaire   +3 more sources

Automated FRAP microscopy for high‐throughput analysis of protein dynamics in chromatin organization and transcription

FEBS Open Bio, EarlyView.
RoboMic is an automated confocal microscopy pipeline for high‐throughput functional imaging in living cells. Demonstrated with fluorescence recovery after photobleaching (FRAP), it integrates AI‐driven nuclear segmentation, ROI selection, bleaching, and analysis.
Selçuk Yavuz, Bart Geverts, Johan A. Slotman, Andrea Sacchetti, Stefan Prekovic, Martin E. van Royen, Adriaan B. Houtsmuller   +6 more
wiley   +1 more source

Defects in Emerin-Nucleoskeleton Binding Disrupt Nuclear Structure and Promote Breast Cancer Cell Motility and Metastasis. [PDF]

Mol Cancer Res, 2021
Liddane AG, McNamara CA, Campbell MC, Mercier I, Holaska JM.   +4 more
europepmc   +1 more source

A light‐triggered Time‐Resolved X‐ray Solution Scattering (TR‐XSS) workflow with application to protein conformational dynamics

FEBS Open Bio, EarlyView.
Time‐resolved X‐ray solution scattering captures how proteins change shape in real time under near‐native conditions. This article presents a practical workflow for light‐triggered TR‐XSS experiments, from data collection to structural refinement. Using a calcium‐transporting membrane protein as an example, the approach can be broadly applied to study ...
Fatemeh Sabzian‐Molaei, Fredrik Orädd, Konstantinos Magkakis, Magnus Andersson   +3 more
wiley   +1 more source

Nuclear physics experiments with ion storage rings

, 2013
In the last two decades a number of nuclear structure and astrophysics experiments were performed at heavy-ion storage rings employing unique experimental conditions offered by such machines.
Simon, H, Heinz, Andreas Martin,, Bosch, F.J.,, Bishop, S.M.,, Sun, B. H., Sun, B.H.,, Kozhuharov, C, Heinz, A, Walker, P. M., Heinz, Andreas Martin, Zhang, Y., Dillmann, I.,, Tu, X.L., Wälker, P.M., Walker, PM, Grisenti, R.E.,, Kozhuharov, C.,, Ma, X. W., Chen, LX, Wälker, P.M.,, Woods, P.J.,, Woods, P.J., Knöbel, R.K., Yamaguchi, Y, Bosch, F, Steck, M.,, Stöhlker, T., Kalantar-Nayestanaki, N., Winckler, N., Ma, X., Lestinsky, M, Nolden, F.,, Simon, H., Yamaguchi, T, Schneider, D., Bishop, S.M., Schneider, D.H.G., St\uf6hlker, T.H., Stöhlker, T.H.,, Chen, L., Chen, L.X.,, Reifarth, R., Ozawa, A, Simon, H.,, Litvinov, Yu.A.,, Heinz, A., W\ue4lker, P.M., Wakasugi, M, Leštinský, M.,, Reifarth, R.,, Steck, M, Woods, P. J., Bosch, Fritz, Geissel, H, Heil, M, Brandau, C, Schneider, D, Yamaguchi, Y.,, Brandau, C., Tu, X. L., Sun, B.H., Chen, L. X., Xu, H.,, Bishop, S., Zhang, Y.H., Ozawa, A.,, Tu, XL, Bosch, F., Bishop, S, Xu, H., Reed, M.W., Winckler, N, Sanjari, M., Woods, P., Chen, L.X., Geissel, H., Weick, H.,, Uesaka, T., Hagmann, S.,, Brandau, C.,, Yamaguchi, T., Grisenti, R., Woods, PJ, Reifarth, R, Blaum, K.,, Knoebel, R., Zhang, YH, Dillmann, I, Grisenti, RE, Walker, P., Nilsson, Thomas,, Knöbel, R.K.,, Dillmann, I., Reed, M.W.,, Geissel, H.,, Yamaguchi, T.,, Stöhlker, T.H., Stöhlker, T, Litvinov, YA, Sun, BH, Litvinov, Yu A., Zhang, Y.,, Litvinov, Yu. A., Kn\uf6bel, R.K., Nolden, F, Steck, M., Ma, X.W.,, Raabe, R.R.,, Heil, M.,, Raabe, R., Uesaka, T, Schneider, D.H.G.,, Hagmann, S, Sun, B., Raabe, Riccardo, Sanjari, M. S., Ozawa, A., Heil, M., Raabe, R.R., Knöbel, R., Bosch, F.J., Xu, H. S., Sanjari, M.S.,, Egelhof, P.,, Kalantar-Nayestanaki, N.,, Nilsson, T., Stoehlker, T., Xu, HS, Reed, MW, Litvinov, Y., Tu, X., Sanjari, MS, Weick, H, Blaum, K, Winckler, N.,, Ma, X.W., Yamaguchi, Y., Reed, M., Lestinsky, M., Leštinsk\ufd, M., Tu, X.L.,, Sanjari, M.S., Knöbel, R, Hagmann, S., Kozhuharov, C., Weick, H., Nilsson, T, Egelhof, P., Blaum, K., Wakasugi, M., Wakasugi, M.,, Grisenti, R.E., Nolden, F., Xu, H.S., Nilsson, Thomas, Egelhof, P, Zhang, Y. H., Grisenti, R. E., Kalantar-Nayestanaki, N, Ma, XW, Litvinov, Yu.A., Reed, M. W., Raabe, R, Uesaka, T.,   +163 more
core   +1 more source

The human origin recognition complex is essential for pre-RC assembly, mitosis, and maintenance of nuclear structure. [PDF]

Elife, 2021
Chou HC, Bhalla K, Demerdesh OE, Klingbeil O, Hanington K, Aganezov S, Andrews P, Alsudani H, Chang K, Vakoc CR, Schatz MC, McCombie WR, Stillman B.   +12 more
europepmc   +1 more source

Evolutionarily divergent DUF4465 domains have a common vitamin B12‐binding function

FEBS Open Bio, EarlyView.
We show that DUF4465 family proteins, widespread across bacteria from gut microbiomes, hydrothermal vents, and soil, share a common vitamin B12‐binding function. These augmented β‐jellyroll proteins bind vitamin B12 via extended loops. Our findings establish sequence‐diverse DUF4465 proteins as a widespread class of B12‐binding proteins, highlighting ...
Charlea Clarke, Michal Banasik, Rokas Juodeikis, Martin J. Warren, Richard W. Pickersgill   +4 more
wiley   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

FEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane, Lea Nikolić, Lorenzo Maraio, Thomas Goiran, Nathan Karpilovsky, Stefano Sellitto, Vangelis Bouris, Jiang‐An Yin, Ronald Melki, Edward A Fon, Adriano Aguzzi, Elena De Cecco   +11 more
wiley   +1 more source

Nuclear magnetic resonance

, 2012
Podeu consultar el llibre complet a: http://hdl.handle.net/2445/32166This article reviews the principles and methods of nuclear magnetic resonance spectroscopy, and gives examples of applications carried out at our Facility, which illustrate the ...
Molins i Montserrat, Mª Antònia, Gairí Tahull, Margarida, Muñoz-Torrero López-Ibarra, Victoria, Gonzalez, Teresa, Feliz Rodenas, Miguel   +4 more
core  

Nuclear structure and direct reaction studies in particle-γ coincidence experiments at the FSU John D. Fox superconducting linear accelerator laboratory

Frontiers in Physics
Since its foundation in the 1960s, the John D. Fox Superconducting Linear Accelerator Laboratory at Florida State University (FSU) pursued research at the forefront of nuclear science.
Mark-Christoph Spieker, Sergio Almaraz-Calderon   +1 more
doaj   +1 more source