J. A. Mendoza

发表

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.

G. Lorimer, P. Horowitz, E. Rogers, 1991, The Journal of biological chemistry.

Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.

G. Lorimer, P. Horowitz, J. A. Mendoza, 1991, The Journal of biological chemistry.

Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers.

P. Horowitz, J. A. Mendoza, 1994, The Journal of biological chemistry.

Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent.

P. Horowitz, J. A. Mendoza, J. L. Martinez, 1995, Biochimica et biophysica acta.

Ligand-induced Conformational Changes of GroEL Are Dependent on the Bound Substrate Polypeptide*

G. Campo, J. A. Mendoza, 1996, The Journal of Biological Chemistry.

On the chaperonin activity of GroEL at heat-shock temperature.

G. Melkani, J. A. Mendoza, G. Zardeneta, 2005, The international journal of biochemistry & cell biology.

The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure

G. Melkani, J. A. Mendoza, G. Zardeneta, 2003, Biometals.

Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.

P. Horowitz, J. A. Mendoza, M. Butler, 1992, The Journal of biological chemistry.

Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures.

G. Lorimer, P. Horowitz, J. A. Mendoza, 1992, The Journal of biological chemistry.

Unassisted refolding of urea unfolded rhodanese.

G. Lorimer, P. Horowitz, E. Rogers, 1991, The Journal of biological chemistry.

Protection of GroEL by its methionine residues against oxidation by hydrogen peroxide.

G. Melkani, J. A. Mendoza, G. Zardeneta, 2006, Biochemical and biophysical research communications.

Hydrogen peroxide induces the dissociation of GroEL into monomers that can facilitate the reactivation of oxidatively inactivated rhodanese.

G. Melkani, J. A. Mendoza, G. Zardeneta, 2004, The international journal of biochemistry & cell biology.

The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide

P. Horowitz, J. A. Mendoza, 1994, Journal of protein chemistry.

The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature.

J. A. Mendoza, P. Dulin, T. Warren, 2000, Cryobiology.

Mutational Analysis of the BPTI Folding Pathway

D. Goldenberg, J. A. Mendoza, Jian-xin Zhang, 1990 .

The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions

J. A. Mendoza, Kevin K Weinberger, Matthew J. Swan, 2016, Biochemistry and biophysics reports.

The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and ATPase Activities at Elevated Temperatures

J. A. Mendoza, C. M. Buckley, Julian L. Ignacio, 2021, BioChem.

GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation.

G. Melkani, J. A. Mendoza, G. Zardeneta, 2002, Biochemical and biophysical research communications.

alpha-Crystallin facilitates the reactivation of hydrogen peroxide-inactivated rhodanese.

J. A. Mendoza, G. Zardeneta, D. Del Fierro, 2000, Biochemical and biophysical research communications.

Divalent cations stabilize GroEL under conditions of oxidative stress.

G. Melkani, J. A. Mendoza, G. Zardeneta, 2008, Biochemical and biophysical research communications.

Oxidized GroEL can function as a chaperonin.

G. Melkani, J. A. Mendoza, G. Zardeneta, 2004, Frontiers in bioscience : a journal and virtual library.

Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.

P. Horowitz, B. Demeler, J. A. Mendoza, 1994, The Journal of biological chemistry.

Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures.

G. Melkani, J. A. Mendoza, G. Zardeneta, 2012, Bioscience reports.

Partially folded rhodanese or its N-terminal sequence can disrupt phospholipid vesicles

P. Horowitz, J. A. Mendoza, Earl Grant, 1993, Journal of protein chemistry.

Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese.

J. Chirgwin, G. Kurzban, S. Hardies, 1992, Biochimica et Biophysica Acta.

The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures.

J. A. Mendoza, P. Dulin, T. Warren, 1996, Biochemical and biophysical research communications.

Sulfhydryl modification ofE. coli cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex

P. Horowitz, J. A. Mendoza, 1992, Journal of protein chemistry.

GTP binds to α-crystallin and causes a significant conformational change.

J. A. Mendoza, G. Zardeneta, Matthew Correa, 2012, International Journal of Biological Macromolecules.

Thermostabilization of enzymes by the chaperonin GroEL

J. A. Mendoza, M. Manson, E. Ackermann, 1996 .