Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Asaf Shemesh"'
Publikováno v:
ACS Omega, Vol 3, Iss 11, Pp 16246-16252 (2018)
Externí odkaz:
https://doaj.org/article/095fac2ebb684502995715ccacf6e80a
Publikováno v:
ACS Chemical Biology. 16:2212-2227
Tubulin self-association is a critical process in microtubule dynamics. The early intermediate structures, energetics, and their regulation by fluxes of chemical energy, associated with guanosine triphosphate (GTP) hydrolysis, are poorly understood.
Autor:
Asaf Shemesh, Nadiv Dharan, Avi Ginsburg, Raviv Dharan, Yael Levi-Kalisman, Israel Ringel, Uri Raviv
Publikováno v:
The journal of physical chemistry letters. 13(41)
Tubulin nucleation is a highly frequent event in microtubule (MT) dynamics but is poorly understood. In this work, we characterized the structural changes during the initial nucleation phase of dynamic tubulin. Using size-exclusion chromatography-elu
Autor:
Abigail Millgram, Ran Zalk, Israel Ringel, Gabriel A. Frank, Uri Raviv, Raviv Dharan, Asaf Shemesh, Yael Levi-Kalisman
Publikováno v:
ACS nano 15(5), 8836-8847 (2021). doi:10.1021/acsnano.1c01374
ACS nano 15(5), 8836 - 8847 (2021). doi:10.1021/acsnano.1c01374
Tubulin, an essential cytoskeletal protein, assembles into various morphologies by interacting with an array of cellular factors. One of these factors is the endogenous polyamine sp
Tubulin, an essential cytoskeletal protein, assembles into various morphologies by interacting with an array of cellular factors. One of these factors is the endogenous polyamine sp
Autor:
Asaf, Shemesh, Hiba, Ghareeb, Raviv, Dharan, Yael, Levi-Kalisman, Norman, Metanis, Israel, Ringel, Uri, Raviv
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1871:140869
We investigated how the self-association of isolated tubulin dimers affects the rate of GTP hydrolysis and the equilibrium of nucleotide exchange. Both reactions are relevant for microtubule (MT) dynamics. We used HPLC to determine the concentrations
Cold tubulin dimers coexist with tubulin oligomers and single-rings. These structures are involved in microtubule assembly, however, their dynamics are poorly understood. Using state-of-the-art solution synchrotron time-resolved small-angle X-ray sca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f569ccbf291be408681dbfd4c857b3f
https://doi.org/10.26434/chemrxiv-2022-93whb
https://doi.org/10.26434/chemrxiv-2022-93whb
Publikováno v:
The Journal of Physical Chemistry C. 123:28486-28493
Gold nanoparticles (AuNPs) have been the focus of many studies owing to their unique optical and electronic properties and versatile applications. However, synthesis of stable and homogeneous AuNPs...
Publikováno v:
ACS omega 3(11), 16246-16252 (2018). doi:10.1021/acsomega.8b01289
ACS Omega
ACS Omega, Vol 3, Iss 11, Pp 16246-16252 (2018)
ACS Omega
ACS Omega, Vol 3, Iss 11, Pp 16246-16252 (2018)
ACS omega 3(11), 16246 - 16252 (2018). doi:10.1021/acsomega.8b01289
Exposure of a protein to cosolutes, like denaturants, changes its folding equilibrium. To determine the ensemble of protein conformations at equilibrium, in the presence of weak
Exposure of a protein to cosolutes, like denaturants, changes its folding equilibrium. To determine the ensemble of protein conformations at equilibrium, in the presence of weak
Publikováno v:
Biochemistry. 57:6153-6165
Single and double tubulin rings were studied under a range of conditions and during microtubule (MT) assembly and disassembly. Here, tubulin was purified from porcine brain and used without any further modifications or additives that promote ring ass
Tubulin dimers are flexible entities serving as building blocks for construction of cellular polymers essential for the cytoskeleton. The conformational state of the dimer dictates the exact formation of assembly and can be regulated by cellular fact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a581b77bf07730d0dc2786355e9da90
https://doi.org/10.26434/chemrxiv.11353166.v1
https://doi.org/10.26434/chemrxiv.11353166.v1