Results 281 to 290 of about 186,109 (312)

The c-Fes Family of Protein-Tyrosine Kinases

Critical Reviews™ in Oncogenesis, 1998
The human c-fes protooncogene encodes a protein-tyrosine kinase (c-Fes) distinct from c-Src, c-Abl and other nonreceptor tyrosine kinases. Although originally identified as the cellular homolog of several transforming retroviral oncoproteins, Fes was later found to exhibit strong expression in myeloid hematopoietic cells and to play a direct role in ...
T E, Smithgall, J A, Rogers, K L, Peters, J, Li, S D, Briggs, J M, Lionberger, H, Cheng, A, Shibata, B, Scholtz, S, Schreiner, N, Dunham   +10 more
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Building Fe–S proteins: bacterial strategies

Nature Reviews Microbiology, 2010
The broad range of cellular activities carried out by Fe-S proteins means that they have a central role in the life of most organisms. At the interface between biology and chemistry, studies of bacterial Fe-S protein biogenesis have taken advantage of the specific approaches of each field and have begun to reveal the molecular mechanisms involved.
Py, Béatrice, Barras, Frédéric
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The Role of Fe Protein in Nitrogenase Catalysis

1985
The role of Fe protein in nitrogenase catalysis seems to be understood (Mortenson, Thorneley, 1979; Hageman, Burris, 1980). Fe protein con­tains a [4Fe-4S] cluster that functions as a one electron donor. Reduced Fe protein, MoFe protein and two MgATP rapidly form a ternary complex.
Haaker, H., Cordewener, J., ten Asbroek, A., Wassink, H., Eady, R.R., Veeger, C.   +5 more
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Fe-S clusters masquerading as zinc finger proteins

Journal of Inorganic Biochemistry, 2022
Metal ions are commonly found as protein co-factors in biology, and it is estimated that over a quarter of all proteins require a metal cofactor. The distribution and utilization of metals in biology has changed over time. As the earth evolved, the atmosphere became increasingly oxygen rich which affected the bioavailability of certain metals such as ...
Jordan D, Pritts, Sarah L J, Michel
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Fe-Fe separation may explain iron protein behavior

Chemical & Engineering News Archive, 2000
The unusually short distance between iron atoms recently discovered in a ferritin intermediate may explain why diiron centers behave so differently in various iron proteins [Science, 287, 122 (2000) ]. Such centers act as catalytic cofactors in oxygen-activating enzymes, for example, but as substrate intermediates in ferritin, the protein that stores ...
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Fe-Protein Fe:S Ligands

1984
We report functional roles for some Av2 (Azotobacter vinelandii Fe-protein) cysteinyl (Cys) residues using the chemical reactivity of the Cys with iodoacetic acid (IAA) as a probe, Cysteinyl residues were modified with [14C]-IAA under a variety of conditions. The percent carboxymethylation for each of the 7 residues (Cys-5, 38, 85, 97, 132, 151 and 184)
Robert P. Hausinger, James Bryant Howard
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X-ray absorption spectroscopy of 3-Fe clusters in FeS proteins

Inorganica Chimica Acta, 1983
Abstract Fe EXAFS and edge spectroscopy have been used to characterize the 3-Fe clusters in aconitase and Azotobacter vinelandii ferredoxin I (Av Fd I). Fe EXAFS of a frozen solution of oxidized (unactivated) beef heart aconitase indicates a ‘compact’ cluster structure with FeFe distances of ca.
R.A. Scott, S.A. Kazmi, H. Beinert, M.H. Emptage, J.E. Hahn, K.O. Hodgson, C.D. Stout, A.J. Thompson   +7 more
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Exchange-coupled Fe-X-Fe model compounds for certain iron proteins

Hyperfine Interactions, 1988
X-ray structure studies, Mossbauer experiments and magnetic susceptibility measurements were used in connection with molecular orbital calculations to monitor structurally induced changes of electronic and magnetic properties in exchangecoupled [Fe2S2 (SR)4]2- and [Fe2OCl6]2- anions.
J. Adler, J. Ensling, P. Gütlich, E. L. Bominaar, J. Guillin, A. X. Trautwein   +5 more
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Chemical and electrochemical interrelationships of the 1-Fe, 2-Fe, and 4-Fe analogs of the active sites of iron-sulfur proteins

Inorganic Chemistry, 1977
Die ein-, zwei- und vier-kernigen Titelkomplexe (I) bis (IV) sind aus einfachen Eisensalzen zuganglich.
J. Cambray, R. W. Lane, A. G. Wedd, Richard W. Johnson, R. H. Holm   +4 more
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The role of Fe–S proteins in sensing and regulation in bacteria

Current Opinion in Microbiology, 2003
Fe-S clusters are key to the sensing and transcription functions of three transcription factors, FNR, IscR and SoxR. All three proteins were discovered in Escherichia coli but experimental data and bioinformatic predictions suggest that homologs of these proteins exist in other bacterial species, highlighting the widespread nature of Fe-S-dependent ...
Patricia J, Kiley, Helmut, Beinert
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