Results 271 to 280 of about 186,109 (312)

Bioavailability of Functional Iron in Protein Microparticles. [PDF]

Nutrients
Chaiwaree S, Georgieva R, Deckart T, Lenz J, Choonukoolphong T, Suriyaprom S, Prapan A, Cheepchirasuk N, Pruß A, Xiong Y, Tragoolpua Y, Bäumler H.   +11 more
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Hypoxic and Fe-Responses are Regulated by the ERFVII Factors and the PCO Branch of the N-Degron Pathway According to Iron Availability. [PDF]

Plant Cell Environ
Telara Y, Maghrebi M, Lavilla-Puerta M, Monaca N, Ambrogini G, Sbrana A, Delucchi S, Perata P, Vigani G, Giuntoli B.   +9 more
europepmc   +1 more source

Phosphorylation of a novel STK substrate SstP1 links SUF Fe-S cluster biogenesis to oxidative stress resistance and virulence in <i>Streptococcus suis</i>. [PDF]

Virulence
Ren S, Yin H, Wang Y, Yan R, Jia X, Li Z, Li Y, Tian Y, Peng L, Li J, Fang R.   +10 more
europepmc   +1 more source

Selective targeting of a histone-like silencer Sfx to the R6K conjugal transfer operon. [PDF]

Nucleic Acids Res
Wang B, Gupta R, Blaine N, Khitiri B, Jordan C, Molotievskiy N, Dunlap D, Finzi L, Artsimovitch I.   +8 more
europepmc   +1 more source

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Electrochemical Studies of the Mono-Fe, Fe−Zn, and Fe−Fe Metalloisoforms of Bacteriophage λ Protein Phosphatase

Biochemistry, 2003
Bacteriophage lambda protein phosphatase (lambdaPP) is a member of a large superfamily of metallophosphoesterases, including serine/threonine protein phosphatases, purple acid phosphatases, 5'-nucleotidase, and DNA repair enzymes such as Mre11. Members of this family share several common characteristics, including a common phosphoesterase motif ...
Tiffany A, Reiter, Frank, Rusnak
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Methods for Heterologous Overproduction of Fe-S Proteins

2021
Proteins carrying iron-sulfur ([Fe-S]) clusters are critical to the basic metabolism of all organisms. Structural and biochemical investigations of many such [Fe-S] cluster proteins depend on recombinant overproduction using heterologous bacterial hosts such as Escherichia coli .
Elliot I, Corless, Edwin, Antony
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Functional Models of [Fe—S] Nitrosyl Proteins.

ChemInform, 2004
AbstractFor Abstract see ChemInform Abstract in Full Text.
N. A. Sanina, S. M. Aldoshin
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Fe-S proteins in sensing and regulatory functions

Current Opinion in Chemical Biology, 1999
In the past five to ten years, it has become increasingly apparent that the function of Fe-S clusters is not limited to electron transfer, a function implicit in their discovery. We now know that the vulnerability of these structures to oxidative destruction is used by nature in sensing O2, iron, and possibly also nitric oxide. Changes in the oxidation
H, Beinert, P J, Kiley
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