Zobrazeno 1 - 10
of 93
pro vyhledávání: '"Larry E. Vickery"'
Publikováno v:
Cancer Research. 70:6004-6014
Activation of the mitogen-activated protein kinase (MAPK) pathway plays a major role in neoplastic cell transformation. Using a proteomics approach, we identified α tubulin and β tubulin as proteins that interact with activated MAP/extracellular si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75baf4dab22a2af6364dad18462c8e3d
https://doi.org/10.1158/0008-5472.can-09-4490
https://doi.org/10.1158/0008-5472.can-09-4490
Autor:
Jin Hae Kim, Marco Tonelli, Anna K. Füzéry, Larry E. Vickery, William M. Westler, John L. Markley, Dennis T. Ta
Publikováno v:
Biochemistry. 48:6062-6071
IscU is a scaffold protein that functions in iron-sulfur cluster assembly and transfer. Its critical importance has been recently underscored by the finding that a single intronic mutation in the human iscu gene is associated with a myopathy resultin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be7312fc62846d272229866e81e879c4
https://doi.org/10.1021/bi9002277
https://doi.org/10.1021/bi9002277
Publikováno v:
Biochemistry. 47:12795-12801
The HscA/HscB chaperone/cochaperone system accelerates transfer of iron-sulfur clusters from the FeS-scaffold protein IscU (IscU(2)[2Fe2S], holo-IscU) to acceptor proteins in an ATP-dependent manner. We have employed visible region circular dichroism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4db396533d290296b6e34bb2e74c497a
https://doi.org/10.1021/bi801565j
https://doi.org/10.1021/bi801565j
Autor:
Gabriel Cornilescu, Larry E. Vickery, Marco Tonelli, John L. Markley, Dennis T. Ta, Anna K. Füzéry
Publikováno v:
Biochemistry
The interaction between IscU and HscB is critical for successful assembly of iron-sulfur clusters. NMR experiments were performed on HscB to investigate which of its residues might be part of the IscU binding surface. Residual dipolar couplings ( (1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de8bca5d994b03a367ff6089f87b85c6
https://doi.org/10.1021/bi800502r
https://doi.org/10.1021/bi800502r
Publikováno v:
Biochemistry. 44:12307-12315
Hsp70-class molecular chaperones interact with diverse polypeptide substrates, but there is limited information on the structures of different Hsp70-peptide complexes. We have used a site-directed fluorescence labeling and quenching strategy to inves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7ccaa87333c9a1cb444bb7467e7d6f3
https://doi.org/10.1021/bi051145r
https://doi.org/10.1021/bi051145r
Publikováno v:
Journal of Biological Chemistry. 280:29513-29518
IscU/Isu and IscA/Isa (and related NifU and SufA proteins) have been proposed to serve as molecular scaffolds for preassembly of [FeS] clusters to be used in the biogenesis of iron-sulfur proteins. In vitro studies demonstrating transfer of preformed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed36d5faeebf697592408e65bb924581
https://doi.org/10.1074/jbc.m504344200
https://doi.org/10.1074/jbc.m504344200
Autor:
Larry E. Vickery, Tim L. Tapley
Publikováno v:
Journal of Biological Chemistry. 279:28435-28442
HscA, a specialized bacterial hsp70-class chaperone, interacts with the iron-sulfur cluster assembly protein IscU by recognizing a conserved LPPVK sequence motif at positions 99-103. We have used a site-directed fluorescence labeling and quenching st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78eaa5e797b6bd22d5457531a88acd88
https://doi.org/10.1074/jbc.m400803200
https://doi.org/10.1074/jbc.m400803200
Publikováno v:
Journal of Biological Chemistry. 279:19551-19558
IscS catalyzes the fragmentation of l-cysteine to l-alanine and sulfane sulfur in the form of a cysteine persulfide in the active site of the enzyme. In Escherichia coli IscS, the active site cysteine Cys(328) resides in a flexible loop that potentia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3409ff8f63e62ca77b4101a42e3748a1
https://doi.org/10.1074/jbc.m401261200
https://doi.org/10.1074/jbc.m401261200
Publikováno v:
Journal of Biological Chemistry. 278:37582-37589
Hsc66 (HscA) and Hsc20 (HscB) from Escherichia coli comprise a specialized chaperone system that selectively binds the iron-sulfur cluster template protein IscU. Hsc66 interacts with peptides corresponding to a discrete region of IscU including resid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6383d220afeb585487727d70b3f27f5e
https://doi.org/10.1074/jbc.m305292200
https://doi.org/10.1074/jbc.m305292200
Publikováno v:
Journal of Molecular Biology. 330:1049-1059
IscS is a widely distributed cysteine desulfurase that catalyzes the pyridoxal phosphate-dependent desulfuration of L-cysteine and plays a central role in the delivery of sulfur to a variety of metabolic pathways. We report the crystal structure of E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92eac8fb18bda48d0bcddc94b08df52b
https://doi.org/10.1016/s0022-2836(03)00690-9
https://doi.org/10.1016/s0022-2836(03)00690-9