| Name | protein is |
|---|---|
| Synonyms | ANX 2; p36; LIP 2; LIP2; ANX2; ANX2L4; ANX2P1; ANX2P2… |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 20176015 | Duschene KS, Broderick JB: The antiviral protein viperin is a radical enzyme. FEBS Lett. 2010 Mar 19;584(6):1263-7. Epub 2010 Feb 20. Viperin, an interferon-inducible antiviral protein, is shown to bind an iron-sulfur cluster, based on iron analysis as well as UV-Vis and electron paramagnetic resonance spectroscopic data. |
81(1,1,1,1) | Details |
| 19820057 | Guttmann RP: Redox regulation of -dependent enzymes. J Anim Sci. 2010 Apr;88(4):1297-306. Epub 2009 Oct 9. One of the primary targets of oxidation within a protein is the AA whose thiol side chain is highly sensitive to all types of oxidizing agents. Whether the damage is due to a pathological condition or to postmortem mediated loss of redox homeostasis, -dependent enzymes are targets of all forms of reactive and sulfur species. |
1(0,0,0,1) | Details |
| 20110690 | Shi S, Notenboom S, Dumont ME, Ballatori N: Identification of human gene products containing Pro-Pro-x-Tyr (PY) motifs that enhance and endocytotic marker uptake in yeast. Cell Physiol Biochem. 2010;25(2-3):293-306. Epub 2010 Jan 12. Five genes capable of rescuing growth on sulfur-deficient GSH-containing medium were identified: prostate transmembrane protein, androgen induced 1 (PMEPA1); lysosomal-associated protein transmembrane 4 alpha (LAPTM4alpha); solute carrier family 25, member 1 (SLC25A1); lipopolysaccharide-induced TNF factor (LITAF); and cysteine/tyrosine-rich-1 (CYYR1). Interestingly, each protein is predicted to contain Pro-Pro-x-Tyr (PY) motifs, which are thought to be important for regulating protein cell surface expression. |
1(0,0,0,1) | Details |
| 19741035 | Alfaro JF, Joswig-Jones CA, Ouyang W, Nichols J, Crouch GJ, Jones JP: Purification and mechanism of human aldehyde oxidase expressed in Escherichia coli. Drug Metab Dispos. 2009 Dec;37(12):2393-8. Epub 2009 Sep 9. The resulting protein is active, with sulfur being incorporated in the cofactor. |
31(0,1,1,1) | Details |
| 20094789 | Tsukatani Y, Wen J, Blankenship RE, Bryant DA: Characterization of the FMO protein from the aerobic chlorophototroph, Candidatus Chloracidobacterium thermophilum. Photosynth Res. 2010 Jan 22. The spectroscopic features of this FMO protein were different from those of the FMO protein of green sulfur bacteria (GSB) and suggested that exciton coupling of the BChls in the FMO protein is weaker than in FMO of GSB especially at room temperature. |
6(0,0,1,1) | Details |
| 19968861 | Poliak P, Van Hoewyk D, Obornik M, Zikova A, Stuart KD, Tachezy J, Pilon M, Lukes J: Functions and cellular localization of cysteine desulfurase and selenocysteine lyase in Trypanosoma brucei. FEBS J. 2010 Jan;277(2):383-93. Epub 2009 Dec 7. Nfs-like proteins have cysteine desulfurase (CysD) activity, which removes sulfur (S) from and provides S for iron-sulfur cluster assembly and the thiolation of tRNAs. A second Nfs-like protein is encoded in the nuclear genome of T. brucei. |
2(0,0,0,2) | Details |
| 19750513 | Baudouin-Cornu P, Lagniel G, Chedin S, Labarre J: Development of a new method for absolute protein quantification on 2-D gels. Proteomics. 2009 Oct;9(20):4606-15. After separation of (35) S-labeled proteins on 2-D gels, each protein is counted. |
1(0,0,0,1) | Details |
| 19429620 | Zhang J, Biswas I: phosphatase activity is required for stress tolerance in Streptococcus mutans. J Bacteriol. 2009 Jul;191(13):4330-40. Epub 2009 May 8. Furthermore, the distribution of homologs of SMU.1297 in streptococci indicates that this protein is essential for stress tolerance in these organisms. Sequence analysis suggests that SMU.1297 encodes a hypothetical protein with a high degree of homology to the Bacillus subtilis YtqI protein, which possesses an oligoribonuclease activity that cleaves nano-RNAs and a phosphatase activity that degrades (pAp) and 3'-phosphoadenosine-5'- (pApS) to produce AMP; the latter activity is similar to the activity of the Escherichia coli CysQ protein, which is required for sulfur assimilation. |
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. UV-Vis absorption and CD spectroscopy, elemental analysis, gel filtration, and analytical ultracentrifugation confirm that the protein is folded and assembled as designed, namely, alpha-helical coiled-coil binding a single Fe (4) S (4) cluster. |
1(0,0,0,1) | Details |
| 20061482 | Grimm F, Cort JR, Dahl C: DsrR, a novel IscA-like protein lacking iron- and Fe-S-binding functions, involved in the regulation of sulfur oxidation in Allochromatium vinosum. J Bacteriol. 2010 Mar;192(6):1652-61. Epub 2010 Jan 8. We used nuclear magnetic resonance (NMR) spectroscopy to solve the solution structure of DsrR and to show that the protein is indeed structurally highly similar to A-type scaffolds. |
1(0,0,0,1) | Details |
| 19747101 | Eprintsev AT, Klimova MA, Shikhalieva KD, Fedorin DN, Dzhaber MT, Kompantseva EI: Features of structural organization and expression regulation of malate dehydrogenase isoforms from Rhodobacter sphaeroides strain 2R. Biochemistry. 2009 Jul;74(7):793-9. Two isoforms of malate dehydrogenase (MDH), dimeric and tetrameric, have been found in the purple non-sulfur bacterium Rhodobacter sphaeroides strain 2R, devoid of the shunt, which assimilate via the cycle. Inhibitory analysis showed that the 74-kDa protein is involved in tricarboxylic acid cycle, while the 148-kDa MDH takes part in the pathway. |
1(0,0,0,1) | Details |
| 20208432 | Zeng J, Liu Q, Zhang X, Mo H, Wang Y, Chen Q, Liu Y: Functional roles of the aromatic residues in the stabilization of the [Fe4S4] cluster in the Iro protein from Acidithiobacillus ferrooxidans. J Microbiol Biotechnol. 2010 Feb;20(2):294-300. The Iro protein is a member of HiPIP family with the [Fe4S4] cluster for electron transfer. Many reports proposed that the conserved aromatic residues might be responsible for the stability of the iron-sulfur cluster in HiPIP. |
1(0,0,0,1) | Details |
| 20004628 | Sayer NM, Whiting R, Green AC, Anderson K, Jenner J, Lindsay CD: Direct binding of sulfur mustard and chloroethyl ethyl sulphide to human cell membrane-associated proteins; implications for sulfur mustard pathology. J Chromatogr B Analyt Technol Biomed Life Sci. 2009 Nov 18. Actin, annexin A2 and keratin 9 were labelled with SM at a higher intensity than was seen with the same concentration of CEES. |
1(0,0,0,1) | Details |
| 19368556 | Neumann M, Mittelstadt G, Iobbi-Nivol C, Saggu M, Lendzian F, Hildebrandt P, Leimkuhler S: A periplasmic oxidoreductase represents the first dinucleotide cofactor containing molybdo-flavoenzyme from Escherichia coli. FEBS J. 2009 May;276(10):2762-74. Epub 2009 Apr 1. Here, we describe the purification and characterization of gene products of the yagTSRQ operon, a -containing iron-sulfur flavoprotein from E. coli, which is located in the periplasm. |
0(0,0,0,0) | Details |