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Similar articles for PubMed (Select 11073985)


A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex.

Eilers AL, Sundwall E, Lin M, Sullivan AA, Ayer DE.

Mol Cell Biol. 2002 Dec;22(24):8514-26.


Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors.

Billin AN, Eilers AL, Queva C, Ayer DE.

J Biol Chem. 1999 Dec 17;274(51):36344-50.


The Mlx network: evidence for a parallel Max-like transcriptional network that regulates energy metabolism.

Billin AN, Ayer DE.

Curr Top Microbiol Immunol. 2006;302:255-78. Review.


Mga, a dual-specificity transcription factor that interacts with Max and contains a T-domain DNA-binding motif.

Hurlin PJ, Steingrìmsson E, Copeland NG, Jenkins NA, Eisenman RN.

EMBO J. 1999 Dec 15;18(24):7019-28. Erratum in: EMBO J 2000 Jul 17;19(14):3841.


Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc.

Gupta K, Anand G, Yin X, Grove L, Prochownik EV.

Oncogene. 1998 Mar 5;16(9):1149-59.


Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation.

Hurlin PJ, Quéva C, Koskinen PJ, Steingrímsson E, Ayer DE, Copeland NG, Jenkins NA, Eisenman RN.

EMBO J. 1995 Nov 15;14(22):5646-59. Erratum in: EMBO J. 1996 Apr 15;15(8):2030.


Transcription activation by Myc and Max: flanking sequences target activation to a subset of CACGTG motifs in vivo.

Fisher F, Crouch DH, Jayaraman PS, Clark W, Gillespie DA, Goding CR.

EMBO J. 1993 Dec 15;12(13):5075-82.


Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells.

Grinberg AV, Hu CD, Kerppola TK.

Mol Cell Biol. 2004 May;24(10):4294-308.


Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?

Meroni G, Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A.

Oncogene. 2000 Jul 6;19(29):3266-77.


Nucleo-cytoplasmic shuttling of Id2, a negative regulator of basic helix-loop-helix transcription factors.

Kurooka H, Yokota Y.

J Biol Chem. 2005 Feb 11;280(6):4313-20. Epub 2004 Nov 24.


Design and properties of a Myc derivative that efficiently homodimerizes.

Soucek L, Helmer-Citterich M, Sacco A, Jucker R, Cesareni G, Nasi S.

Oncogene. 1998 Nov 12;17(19):2463-72.


The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control.

Brownlie P, Ceska T, Lamers M, Romier C, Stier G, Teo H, Suck D.

Structure. 1997 Apr 15;5(4):509-20.


Dynamic in vivo interactions among Myc network members.

Yin X, Landay MF, Han W, Levitan ES, Watkins SC, Levenson RM, Farkas DL, Prochownik EV.

Oncogene. 2001 Aug 2;20(34):4650-64.


Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor.

Meroni G, Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter DH, Brent R, Ballabio A, Carrozzo R.

EMBO J. 1997 May 15;16(10):2892-906. Erratum in: EMBO J 1997 Oct 1;16(19):6055.


Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo.

Grandori C, Mac J, Siëbelt F, Ayer DE, Eisenman RN.

EMBO J. 1996 Aug 15;15(16):4344-57.


Mad proteins contain a dominant transcription repression domain.

Ayer DE, Laherty CD, Lawrence QA, Armstrong AP, Eisenman RN.

Mol Cell Biol. 1996 Oct;16(10):5772-81.


Lack of transcriptional repression by max homodimers.

Yin X, Grove L, Prochownik EV.

Oncogene. 1998 May;16(20):2629-37.

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