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Items: 14

1.

Antigen clasping by two antigen-binding sites of an exceptionally specific antibody for histone methylation.

Hattori T, Lai D, Dementieva IS, Montaño SP, Kurosawa K, Zheng Y, Akin LR, Świst-Rosowska KM, Grzybowski AT, Koide A, Krajewski K, Strahl BD, Kelleher NL, Ruthenburg AJ, Koide S.

Proc Natl Acad Sci U S A. 2016 Feb 23;113(8):2092-7. doi: 10.1073/pnas.1522691113. Epub 2016 Feb 9.

2.

SUMO modification of cell surface Kv2.1 potassium channels regulates the activity of rat hippocampal neurons.

Plant LD, Dowdell EJ, Dementieva IS, Marks JD, Goldstein SA.

J Gen Physiol. 2011 May;137(5):441-54. doi: 10.1085/jgp.201110604.

3.

One SUMO is sufficient to silence the dimeric potassium channel K2P1.

Plant LD, Dementieva IS, Kollewe A, Olikara S, Marks JD, Goldstein SA.

Proc Natl Acad Sci U S A. 2010 Jun 8;107(23):10743-8. doi: 10.1073/pnas.1004712107. Epub 2010 May 24.

4.

Pentameric assembly of potassium channel tetramerization domain-containing protein 5.

Dementieva IS, Tereshko V, McCrossan ZA, Solomaha E, Araki D, Xu C, Grigorieff N, Goldstein SA.

J Mol Biol. 2009 Mar 20;387(1):175-91. doi: 10.1016/j.jmb.2009.01.030. Epub 2009 Jan 23.

5.
6.

Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the mutation of Tyrosine 72 to phenylalanine, and its mechanistic consequences.

Kulikova VV, Zakomirdina LN, Dementieva IS, Phillips RS, Gollnick PD, Demidkina TV, Faleev NG.

Biochim Biophys Acta. 2006 Apr;1764(4):750-7. Epub 2006 Jan 3.

PMID:
16455316
7.

Role of arginine 226 in the mechanism of tryptophan indole-lyase from Proteus vulgaris.

Kulikova VV, Zakomirdina LN, Bazhulina NP, Dementieva IS, Faleev NG, Gollnick PD, Demidkina TV.

Biochemistry (Mosc). 2003 Nov;68(11):1181-8.

8.

Role of aspartate-133 and histidine-458 in the mechanism of tryptophan indole-lyase from Proteus vulgaris.

Demidkina TV, Zakomirdina LN, Kulikova VV, Dementieva IS, Faleev NG, Ronda L, Mozzarelli A, Gollnick PD, Phillips RS.

Biochemistry. 2003 Sep 30;42(38):11161-9.

PMID:
14503866
9.

Tryptophan indole-lyase from Proteus vulgaris: kinetic and spectral properties.

Zakomirdina LN, Kulikova VV, Gogoleva OI, Dementieva IS, Faleev NG, Demidkina TV.

Biochemistry (Mosc). 2002 Oct;67(10):1189-96.

10.
11.

Crystal structure of tryptophanase.

Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH.

J Mol Biol. 1998 Feb 27;276(3):603-23.

PMID:
9551100
12.

2-Methyl-L-tryptophan is a substrate of tryptophanase.

Faleev NG, Gogoleva OI, Dementieva IS, Zakomirdina LN, Belikov VM.

Biochem Mol Biol Int. 1995 Apr;35(5):1037-40.

PMID:
7549921
13.

Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents.

Faleev NG, Dementieva IS, Zakomirdina LN, Gogoleva OI, Belikov VM.

Biochem Mol Biol Int. 1994 Aug;34(1):209-16.

PMID:
7849621
14.

Crystallization and preliminary X-ray investigation of holotryptophanases from Escherichia coli and Proteus vulgaris.

Dementieva IS, Zakomirdina LN, Sinitzina NI, Antson AA, Wilson KS, Isupov MN, Lebedev AA, Harutyunyan EH.

J Mol Biol. 1994 Jan 14;235(2):783-6.

PMID:
8289300

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