| Name | apoproteins |
|---|---|
| Synonyms | AD2; APOE; Apo E; Apolipoprotein E; Apolipoprotein E precursor; apoprotein; Apo Es; Apolipoprotein Es… |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19348893 | Amutha B, Gordon DM, Dancis A, Pain D: Chapter 14 Nucleotide-dependent iron-sulfur cluster biogenesis of endogenous and imported apoproteins in isolated intact mitochondria. Methods Enzymol. 2009;456:247-66. |
82(1,1,1,2) | Details |
| 19865480 | Xu XM, Lin H, Latijnhouwers M, Moller SG: Dual localized AtHscB involved in iron sulfur protein biogenesis in Arabidopsis. PLoS One. 2009 Oct 29;4(10):e7662. Although simple in structure both the assembly and insertion of clusters into apoproteins requires complex biochemical pathways involving a diverse set of proteins. |
1(0,0,0,1) | Details |
| 20018187 | Czech I, Silakov A, Lubitz W, Happe T: The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor. FEBS Lett. 2010 Feb 5;584(3):638-42. Epub 2009 Dec 14. CaHydF was able to activate Chlamydomonas reinhardtii [FeFe] hydrogenase apoprotein (CrHydA1 (apo)) to almost 100% compared to the native specific evolution activity. |
1(0,0,0,1) | Details |
| 19348891 | Stehling O, Sheftel AD, Lill R: Chapter 12 Controlled expression of iron-sulfur cluster assembly components for respiratory chain complexes in mammalian cells. Methods Enzymol. 2009;456:209-31. Both the synthesis of Fe/S clusters and their delivery to apoproteins depend on the concerted function of specialized, often dedicated, proteins located in the mitochondria and cytosol of eukaryotes. |
1(0,0,0,1) | Details |
| 20060739 | Sheftel A, Stehling O, Lill R: -sulfur proteins in health and disease. Trends Endocrinol Metab. 2010 Jan 7. The past decade has led to the discovery of novel Fe/S proteins and insights into how their Fe/S cofactors are formed and incorporated into apoproteins. |
1(0,0,0,1) | Details |
| 19385603 | Urzica E, Pierik AJ, Muhlenhoff U, Lill R: Crucial role of conserved residues in the assembly of two iron-sulfur clusters on the CIA protein Nar1. Biochemistry. 2009 Jun 9;48(22):4946-58. The CIA protein Nar1 performs a specific function in transferring an Fe/S cluster that is assembled de novo on the Cfd1-Nbp35 scaffold to apoproteins. |
1(0,0,0,1) | Details |
| 19366265 | Gupta V, Sendra M, Naik SG, Chahal HK, Huynh BH, Outten FW, Fontecave M, Ollagnier de Choudens S: Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. J Am Chem Soc. 2009 May 6;131(17):6149-53. Furthermore, native [2Fe-2S] SufA can transfer its Fe-S cluster to both [2Fe-2S] and [4Fe-4S] apoproteins. |
1(0,0,0,1) | Details |
| 20035711 | Grzyb J, Xu F, Weiner L, Reijerse EJ, Lubitz W, Nanda V, Noy D: De novo design of a non-natural fold for an iron-sulfur protein: alpha-helical coiled-coil with a four-iron four-sulfur cluster binding site in its central core. Biochim Biophys Acta. 2010 Mar;1797(3):406-13. Epub 2009 Dec 24. The apoprotein, recombinantly expressed and purified from E. coli, readily self-assembles with Fe (4) S (4) clusters in vitro. |
1(0,0,0,1) | Details |
| 19675643 | Lill R: Function and biogenesis of iron- proteins. Nature. 2009 Aug 13;460(7257):831-8. Despite the relative simplicity of Fe-S clusters in terms of structure and composition, their synthesis and assembly into apoproteins is a highly complex and coordinated process in living cells. |
1(0,0,0,1) | Details |
| 19821612 | Reyda MR, Fugate CJ, Jarrett JT: A complex between synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly. Biochemistry. 2009 Nov 17;48(45):10782-92. We propose that HscA plays a role in facilitating the transfer of FeS clusters from IscU into the appropriate target apoproteins such as synthase, perhaps by enhancing or prolonging the requisite protein-protein interaction. |
1(0,0,0,1) | Details |
| 19528951 | Pierik AJ, Netz DJ, Lill R: Analysis of iron-sulfur protein maturation in eukaryotes. Nat Protoc. 2009;4(5):753-66. The biosynthesis of the inorganic Fe/S centers and their insertion into apoproteins require complex cellular machinery located in the mitochondria (Fe/S cluster (ISC) assembly machinery systems) and cytosol (cytosolic Fe/S protein assembly (CIA) systems). |
1(0,0,0,1) | Details |
| 19817716 | Schwenkert S, Netz DJ, Frazzon J, Pierik AJ, Bill E, Gross J, Lill R, Meurer J: Chloroplast HCF101 is a scaffold protein for [4Fe-4S] cluster assembly. Biochem J. 2009 Dec 14;425(1):207-14. -evolving chloroplasts possess their own iron-sulfur cluster assembly proteins including members of the SUF (sulfur mobilization) and the NFU family. We further demonstrate that the reconstituted cluster is transiently bound and can be transferred from HCF101 to a [4Fe-4S] apoprotein. |
1(0,0,0,1) | Details |
| 19855833 | Kuchenreuther JM, Stapleton JA, Swartz JR: and stimulate in vitro [FeFe] hydrogenase activation. PLoS One. 2009 Oct 26;4(10):e7565. The maturation system is comprised of purified hydrogenase apoprotein; a dialyzed Escherichia coli cell lysate containing heterologous HydE, HydF, and HydG maturases; and exogenous small molecules. |
1(0,0,0,1) | Details |
| 19954209 | Crack JC, den Hengst CD, Jakimowicz P, Subramanian S, Johnson MK, Buttner MJ, Thomson AJ, Le Brun NE: Characterization of [4Fe-4S]-containing and cluster-free forms of Streptomyces WhiD. Biochemistry. 2009 Dec 29;48(51):12252-64. WhiD, a member of the WhiB-like (Wbl) family of iron-sulfur proteins found exclusively within the actinomycetes, is required for the late stages of sporulation in Streptomyces coelicolor. |
0(0,0,0,0) | Details |