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Items: 1 to 20 of 91


Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor.

Brosey CA, Ho C, Long WZ, Singh S, Burnett K, Hura GL, Nix JC, Bowman GR, Ellenberger T, Tainer JA.

Structure. 2016 Dec 6;24(12):2067-2079. doi: 10.1016/j.str.2016.09.012. Epub 2016 Nov 3.


Redox-linked conformational dynamics in apoptosis-inducing factor.

Sevrioukova IF.

J Mol Biol. 2009 Jul 31;390(5):924-38. doi: 10.1016/j.jmb.2009.05.013. Epub 2009 May 15.


Key Role of the Adenylate Moiety and Integrity of the Adenylate-Binding Site for the NAD(+)/H Binding to Mitochondrial Apoptosis-Inducing Factor.

Sorrentino L, Calogero AM, Pandini V, Vanoni MA, Sevrioukova IF, Aliverti A.

Biochemistry. 2015 Dec 1;54(47):6996-7009. doi: 10.1021/acs.biochem.5b00898. Epub 2015 Nov 16.


Poly(ADP-ribose) (PAR) binding to apoptosis-inducing factor is critical for PAR polymerase-1-dependent cell death (parthanatos).

Wang Y, Kim NS, Haince JF, Kang HC, David KK, Andrabi SA, Poirier GG, Dawson VL, Dawson TM.

Sci Signal. 2011 Apr 5;4(167):ra20. doi: 10.1126/scisignal.2000902.


Key Residues Regulating the Reductase Activity of the Human Mitochondrial Apoptosis Inducing Factor.

Villanueva R, Ferreira P, Marcuello C, Usón A, Miramar MD, Peleato ML, Lostao A, Susin SA, Medina M.

Biochemistry. 2015 Aug 25;54(33):5175-84. doi: 10.1021/acs.biochem.5b00696. Epub 2015 Aug 13.


Structural bases of the altered catalytic properties of a pathogenic variant of apoptosis inducing factor.

Sorrentino L, Cossu F, Milani M, Aliverti A, Mastrangelo E.

Biochem Biophys Res Commun. 2017 Aug 26;490(3):1011-1017. doi: 10.1016/j.bbrc.2017.06.156. Epub 2017 Jun 27.


Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor.

Ferreira P, Villanueva R, Martínez-Júlvez M, Herguedas B, Marcuello C, Fernandez-Silva P, Cabon L, Hermoso JA, Lostao A, Susin SA, Medina M.

Biochemistry. 2014 Jul 1;53(25):4204-15. doi: 10.1021/bi500343r. Epub 2014 Jun 20.


Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2).

Elguindy MM, Nakamaru-Ogiso E.

J Biol Chem. 2015 Aug 21;290(34):20815-26. doi: 10.1074/jbc.M115.641498. Epub 2015 Jun 10.


Apoptosis-inducing factor: structure, function, and redox regulation.

Sevrioukova IF.

Antioxid Redox Signal. 2011 Jun 15;14(12):2545-79. doi: 10.1089/ars.2010.3445. Epub 2011 Mar 10. Review.


Nondegradative ubiquitination of apoptosis inducing factor (AIF) by X-linked inhibitor of apoptosis at a residue critical for AIF-mediated chromatin degradation.

Lewis EM, Wilkinson AS, Davis NY, Horita DA, Wilkinson JC.

Biochemistry. 2011 Dec 27;50(51):11084-96. doi: 10.1021/bi201483g. Epub 2011 Dec 2.


Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states.

Winkler A, Udvarhelyi A, Hartmann E, Reinstein J, Menzel A, Shoeman RL, Schlichting I.

J Mol Biol. 2014 Feb 20;426(4):853-68. doi: 10.1016/j.jmb.2013.11.018. Epub 2013 Nov 27.


NADH oxidase activity of mitochondrial apoptosis-inducing factor.

Miramar MD, Costantini P, Ravagnan L, Saraiva LM, Haouzi D, Brothers G, Penninger JM, Peleato ML, Kroemer G, Susin SA.

J Biol Chem. 2001 May 11;276(19):16391-8. Epub 2001 Feb 13.


The crystal structure of the mouse apoptosis-inducing factor AIF.

Maté MJ, Ortiz-Lombardía M, Boitel B, Haouz A, Tello D, Susin SA, Penninger J, Kroemer G, Alzari PM.

Nat Struct Biol. 2002 Jun;9(6):442-6.


Redox reactions of the FAD-containing apoptosis-inducing factor (AIF) with quinoidal xenobiotics: a mechanistic study.

Misevičienė L, Anusevičius Z, Sarlauskas J, Sevrioukova IF, Cėnas N.

Arch Biochem Biophys. 2011 Aug 15;512(2):183-9. doi: 10.1016/ Epub 2011 Jun 2.


Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g).

Kim JT, Kim KD, Song EY, Lee HG, Kim JW, Kim JW, Chae SK, Kim E, Lee MS, Yang Y, Lim JS.

FEBS Lett. 2006 Nov 27;580(27):6375-83. Epub 2006 Nov 3.


Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor.

Ghezzi D, Sevrioukova I, Invernizzi F, Lamperti C, Mora M, D'Adamo P, Novara F, Zuffardi O, Uziel G, Zeviani M.

Am J Hum Genet. 2010 Apr 9;86(4):639-49. doi: 10.1016/j.ajhg.2010.03.002. Epub 2010 Apr 1.


Redox-dependent changes in molecular properties of mitochondrial apoptosis-inducing factor.

Churbanova IY, Sevrioukova IF.

J Biol Chem. 2008 Feb 29;283(9):5622-31. doi: 10.1074/jbc.M709147200. Epub 2007 Dec 31.


Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases.

Maurus R, Nguyen NT, Stokell DJ, Ayed A, Hultin PG, Duckworth HW, Brayer GD.

Biochemistry. 2003 May 20;42(19):5555-65.


X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing.

Sickmier EA, Brekasis D, Paranawithana S, Bonanno JB, Paget MS, Burley SK, Kielkopf CL.

Structure. 2005 Jan;13(1):43-54.


Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.

Meisburger SP, Taylor AB, Khan CA, Zhang S, Fitzpatrick PF, Ando N.

J Am Chem Soc. 2016 May 25;138(20):6506-16. doi: 10.1021/jacs.6b01563. Epub 2016 May 12.

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