Lista de obras - Hui Lu - Dominio Público Uruguay

Acceleration of the folding of hen lysozyme by trifluoroethanol

artículo científico publicado en 1997

Allosteric and electrostatic protein-protein interactions regulate the assembly of the heterohexameric Tim9-Tim10 complex.

artículo científico publicado en 2008

Antibody-Free Discrimination of Protein Biomarkers in Human Serum Based on Surface-Enhanced Raman Spectroscopy

artículo científico publicado en 2018

Assembly of Tim9 and Tim10 into a functional chaperone.

artículo científico publicado en 2002

Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.

artículo científico publicado en 2009

Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1

artículo científico publicado en 2020

Folding and biogenesis of mitochondrial small Tim proteins.

artículo científico publicado en 2013

Frequency Shifts in Surface-Enhanced Raman Spectroscopy-Based Immunoassays: Mechanistic Insights and Application in Protein Carbonylation Detection

scientific article published on 12 July 2019

Functional TIM10 chaperone assembly is redox-regulated in vivo.

artículo científico publicado en 2004

Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10.

artículo científico publicado en 2003

Killing activity of neutrophils is mediated through activation of proteases by K+ flux

artículo científico publicado en 2002

Kinetic characterisation of Erv1, a key component for protein import and folding in yeast mitochondria

artículo científico publicado en 2019

Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.

artículo científico publicado en 2008

Manipulating the folding of membrane proteins: using the bilayer to our advantage

artículo científico publicado en 2001

Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.

artículo científico publicado en 2015

Mitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles.

artículo científico publicado en 2014

Oxidative folding competes with mitochondrial import of the small Tim proteins.

artículo científico publicado en 2008

Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria

artículo científico publicado en 2019

Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function

artículo científico publicado en 2015

Surface-Enhanced Raman Scattering for Direct Protein Function Investigation: Controlled Immobilization and Orientation

artículo científico publicado en 2019

Temperature-dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9-Tim10 complex.

artículo científico publicado en 2011

The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction

artículo científico publicado en 2014

The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH 1 1Edited by A. R. Fersht

artículo científico publicado en 2000

The structural basis of the TIM10 chaperone assembly.

artículo científico publicado en 2004

Zinc binding of Tim10: evidence for existence of an unstructured binding intermediate for a zinc finger protein

scientific article published on 01 April 2008

Zinc can play chaperone-like and inhibitor roles during import of mitochondrial small Tim proteins.

artículo científico publicado en 2008

Lista de obras de Hui Lu

Acceleration of the folding of hen lysozyme by trifluoroethanol

Allosteric and electrostatic protein-protein interactions regulate the assembly of the heterohexameric Tim9-Tim10 complex.

Antibody-Free Discrimination of Protein Biomarkers in Human Serum Based on Surface-Enhanced Raman Spectroscopy

Assembly of Tim9 and Tim10 into a functional chaperone.

Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.

Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1

Folding and biogenesis of mitochondrial small Tim proteins.

Frequency Shifts in Surface-Enhanced Raman Spectroscopy-Based Immunoassays: Mechanistic Insights and Application in Protein Carbonylation Detection

Functional TIM10 chaperone assembly is redox-regulated in vivo.

Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10.

Killing activity of neutrophils is mediated through activation of proteases by K+ flux

Kinetic characterisation of Erv1, a key component for protein import and folding in yeast mitochondria

Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.

Manipulating the folding of membrane proteins: using the bilayer to our advantage

Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.

Mitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles.

Oxidative folding competes with mitochondrial import of the small Tim proteins.

Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria

Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function

Surface-Enhanced Raman Scattering for Direct Protein Function Investigation: Controlled Immobilization and Orientation

Temperature-dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9-Tim10 complex.

The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction

The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH 1 1Edited by A. R. Fersht

The structural basis of the TIM10 chaperone assembly.

Zinc binding of Tim10: evidence for existence of an unstructured binding intermediate for a zinc finger protein

Zinc can play chaperone-like and inhibitor roles during import of mitochondrial small Tim proteins.