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Acta Veterinaria Hungarica|January 1, 1992
Early damages to lung capillaries in enzootic pneumonia of rabbitsC Iregui, J A MendozaThe Journal of Biological Chemistry|October 21, 1994
Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomersJ A Mendoza, P M HorowitzJournal of Protein Chemistry|December 1, 1992
Sulfhydryl modification of E. coli Cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complexJ A Mendoza, P M HorowitzUndersea & Hyperbaric Medicine : Journal of the Undersea and Hyperbaric Medical Society, Inc|February 6, 2007
Epidemiology of severe carbon monoxide poisoning in childrenJ A Mendoza, N B HampsonJournal of Protein Chemistry|January 1, 1994
The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptideJ A Mendoza, P M HorowitzThe Journal of Biological Chemistry|July 5, 1996
Ligand-induced conformational changes of GroEL are dependent on the bound substrate polypeptideJ A Mendoza, G D CampoCryobiology|February 27, 2001
The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperatureJ A Mendoza, P Dulin, T WarrenBiochemical and Biophysical Research Communications|December 4, 1996
The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperaturesJ A Mendoza, T Warren, P DulinBiochemical and Biophysical Research Communications|July 29, 2000
alpha-Crystallin facilitates the reactivation of hydrogen peroxide-inactivated rhodaneseD Del Fierro, G Zardeneta, J A MendozaThe Journal of Biological Chemistry|January 28, 1994
Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin actionJ A Mendoza, B Demeler, P M HorowitzPageof 6