Rojo-Domínguez A - Search Results

1

Stability parameters for one-step mechanism of irreversible protein denaturation: a method based on nonlinear regression of calorimetric peaks with nonzero deltaCp.

Arroyo-Reyna A, Tello-Solís SR, Rojo-Domínguez A. Arroyo-Reyna A, et al. Anal Biochem. 2004 May 15;328(2):123-30. doi: 10.1016/j.ab.2004.02.021. Anal Biochem. 2004. PMID: 15113687

2

pH dependence of the activation parameters for chymopapain unfolding: influence of ion pairs on the kinetic stability of proteins.

Solís-Mendiola S, Gutiérrez-González LH, Arroyo-Reyna A, Padilla-Zúñiga J, Rojo-Domínguez A, Hernández-Arana A. Solís-Mendiola S, et al. Biochim Biophys Acta. 1998 Nov 10;1388(2):363-72. doi: 10.1016/s0167-4838(98)00195-2. Biochim Biophys Acta. 1998. PMID: 9858767

3

Differential scanning calorimetry of the irreversible denaturation of Escherichia coli glucosamine-6-phosphate deaminase.

Hernández-Arana A, Rojo-Domínguez A, Altamirano MM, Calcagno ML. Hernández-Arana A, et al. Biochemistry. 1993 Apr 13;32(14):3644-8. doi: 10.1021/bi00065a017. Biochemistry. 1993. PMID: 8466906

4

Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: evidence of dimerization coupled to refolding of the thermally unfolded protein.

Benítez-Cardoza CG, Rojo-Domínguez A, Hernández-Arana A. Benítez-Cardoza CG, et al. Biochemistry. 2001 Jul 31;40(30):9049-58. doi: 10.1021/bi010528w. Biochemistry. 2001. PMID: 11467968

5

Spectroscopic and thermodynamic evidence for a complex denaturation mechanism of bovine beta-lactoglobulin A.

García-Hernández E, Hernández-Arana A, Zubillaga RA, Rojo-Domínguez A. García-Hernández E, et al. Biochem Mol Biol Int. 1998 Jul;45(4):761-8. doi: 10.1080/15216549800203172. Biochem Mol Biol Int. 1998. PMID: 9713699

6

The thermal unfolding of hevein, a small disulfide-rich protein.

Hernández-Arana A, Rojo-Domínguez A, Soriano-García M, Rodríguez-Romero A. Hernández-Arana A, et al. Eur J Biochem. 1995 Mar 15;228(3):649-52. doi: 10.1111/j.1432-1033.1995.tb20304.x. Eur J Biochem. 1995. PMID: 7737158 Free article.

7

Thermal denaturation of glutathione reductase from cyanobacterium Spirulina maxima.

Rojo-Domínguez A, Hernández-Arana A, Mendoza-Hernández G, Rendón JL. Rojo-Domínguez A, et al. Biochem Mol Biol Int. 1997 Jul;42(3):631-9. doi: 10.1080/15216549700203041. Biochem Mol Biol Int. 1997. PMID: 9247721

8

Loosely packed papain prosegment displays inhibitory activity.

Gutiérrez-González LH, Rojo-Domínguez A, Cabrera-González NE, Pérez-Montfort R, Padilla-Zúñiga AJ. Gutiérrez-González LH, et al. Arch Biochem Biophys. 2006 Feb 15;446(2):151-60. doi: 10.1016/j.abb.2005.12.005. Epub 2005 Dec 29. Arch Biochem Biophys. 2006. PMID: 16427023

9

Unfolding behavior of human alpha 1-acid glycoprotein is compatible with a loosely folded region in its polypeptide chain.

Rojo-Domínguez A, Zubillaga-Luna R, Hernández-Arana A. Rojo-Domínguez A, et al. Biochemistry. 1990 Sep 18;29(37):8689-95. doi: 10.1021/bi00489a026. Biochemistry. 1990. PMID: 2271550

10

Cooperativity in the unfolding transitions of cysteine proteinases. Calorimetric study of the heat denaturation of chymopapain and papain.

Solís-Mendiola S, Rojo-Domínguez A, Hernández-Arana A. Solís-Mendiola S, et al. Biochim Biophys Acta. 1993 Nov 10;1203(1):121-5. doi: 10.1016/0167-4838(93)90045-s. Biochim Biophys Acta. 1993. PMID: 8218380

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