Protein Information

Name protein is
Synonyms ANX 2; p36; LIP 2; LIP2; ANX2; ANX2L4; ANX2P1; ANX2P2…

Compound Information

Name sulfoxide
CAS 5-[2-(octylsulfinyl)propyl]-1,3-benzodioxole

Reference List

PubMed Abstract RScore(About this table)
19902913 Choi S, Jeong J, Na S, Lee HS, Kim HY, Lee KJ, Paek E: New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra. J Proteome Res. 2010 Jan;9(1):626-35.


Identifying the sites of disulfide bonds in a protein is essential for thorough understanding of a protein's tertiary and quaternary structures and its biological functions.
2(0,0,0,2) Details
17511600 Paul S: Polyglutamine-mediated neurodegeneration: use of chaperones as prevention strategy. Biochemistry. 2007 Apr;72(4):359-66.


Clinical studies have revealed that the forming of neuronal intranuclear inclusions by the disease protein is a common pathological feature of polyglutamine diseases.
1(0,0,0,1) Details
18651754 Quinternet M, Tsan P, Neiers F, Beaufils C, Boschi-Muller S, Averlant-Petit MC, Branlant G, Cung MT: Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis. Biochemistry. 2008 Aug 19;47(33):8577-89. Epub 2008 Jul 24.


PilB protein is composed of three domains.
1(0,0,0,1) Details
19049972 Le DT, Lee BC, Marino SM, Zhang Y, Fomenko DE, Kaya A, Hacioglu E, Kwak GH, Koc A, Kim HY, Gladyshev VN: Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae. J Biol Chem. 2009 Feb 13;284(7):4354-64. Epub 2008 Dec 2.

MsrA and MsrB are the best known Msrs that repair methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO) residues in proteins, respectively.
This protein is present in single copies and two mutually exclusive subtypes in about half of prokaryotes and unicellular eukaryotes but is missing in higher plants and animals.
1(0,0,0,1) Details
19494032 Jenny MJ, Karchner SI, Franks DG, Woodin BR, Stegeman JJ, Hahn ME: Distinct roles of two zebrafish AHR repressors (AHRRa and AHRRb) in embryonic development and regulating the response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. Toxicol Sci. 2009 Aug;110(2):426-41. Epub 2009 Jun 3.


The aryl hydrocarbon receptor (AHR) repressor (AHRR), an AHR-related basic helix-loop-helix/Per-AHR nuclear translocator-Sim protein, is regulated by an AHR-dependent mechanism and acts as a transcriptional repressor of AHR function.
1(0,0,0,1) Details
17718518 Boys BL, Kuprowski MC, Konermann L: Symmetric behavior of hemoglobin alpha- and beta- subunits during acid-induced denaturation observed by electrospray mass spectrometry. Biochemistry. 2007 Sep 18;46(37):10675-84. Epub 2007 Aug 24.

The extent of these modifications for freshly prepared protein is lower by at least a factor of 10.
Liquid chromatography and tandem mass spectrometry reveal significant levels of sulfoxide formation for all four methionine residues in commercially obtained metHb.
1(0,0,0,1) Details
18576452 Ludwig C, Michiels PJ, Lodi A, Ride J, Bunce C, Gunther UL: Evaluation of solvent accessibility epitopes for different dehydrogenase inhibitors. ChemMedChem. 2008 Sep;3(9):1371-6.


Knowledge about the orientation of ligands or inhibitors bound to a protein is vital for the development of new drugs.
1(0,0,0,1) Details
18672911 Medower C, Wen L, Johnson WW: Cytochrome P450 oxidation of the thiophene-containing anticancer drug 3-[(quinolin-4-ylmethyl)-amino]-thiophene-2-carboxylic acid (4-trifluoromethoxy-phenyl)-amide to an electrophilic intermediate. Chem Res Toxicol. 2008 Aug;21(8):1570-7. Epub 2008 Aug 2.

The investigational anticancer agent 3-[(quinolin-4-ylmethyl)-amino]-thiophene-2-carboxylic acid (4-trifluoromethoxy-phenyl)-amide (OSI-930) contains a thiophene moiety that can be oxidized by P450s to an apparent sulfoxide, which can react via Michael-addition to the 5-position of the thiophene ring, as demonstrated by mass spectral characterization of several thioether conjugates of the presumed thiophene S-oxide.
The retention of covalent protein adducts of radio-labeled intermediate rat tissue has a half-life of about 1-1.5 days; hence, modified protein is cleared and replaced relatively quickly.
1(0,0,0,1) Details