Lista de obras - Erik Martinez-Hackert - Dominio Público Uruguay

Characterization of the ligand binding functionality of the extracellular domain of activin receptor type IIb.

artículo científico publicado en 2010

Crystal structure of a potassium ion transporter, TrkH

artículo científico publicado en 2011

Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB

artículo científico publicado en 1995

Determination of half-maximal inhibitory concentration using biosensor-based protein interaction analysis

artículo científico publicado en 2016

Distinct molecular mechanisms account for the specificity of two different T-cell receptors

artículo científico publicado en 2003

How a T Cell Receptor-like Antibody Recognizes Major Histocompatibility Complex-bound Peptide

artículo científico publicado en 2008

Human Cerberus prevents nodal-receptor binding, inhibits nodal signaling, and suppresses nodal-mediated phenotypes

artículo científico publicado en 2015

Kinetics of quinine-deuterohemin binding

scientific article published on 01 August 1993

New Ligand Binding Function of Human Cerberus and Role of Proteolytic Processing in Regulating Ligand-Receptor Interactions and Antagonist Activity.

artículo científico publicado en 2016

Orientation of OmpR monomers within an OmpR:DNA complex determined by DNA affinity cleaving 1 1Edited by K. Yamamoto

artículo científico publicado en 1999

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

artículo científico publicado en 2009

Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes.

artículo científico publicado en 1995

Specificity and Structure of a High Affinity Activin Receptor-like Kinase 1 (ALK1) Signaling Complex

artículo científico publicado en 2012

Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26

artículo científico publicado en 2011

Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis

artículo científico publicado en 1993

The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor

artículo científico publicado en 1997

Transforming Growth Factor-β Family Ligands Can Function as Antagonists by Competing for Type II Receptor Binding.

artículo científico publicado en 2016

Lista de obras de Erik Martinez-Hackert

Characterization of the ligand binding functionality of the extracellular domain of activin receptor type IIb.

Crystal structure of a potassium ion transporter, TrkH

Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB

Determination of half-maximal inhibitory concentration using biosensor-based protein interaction analysis

Distinct molecular mechanisms account for the specificity of two different T-cell receptors

How a T Cell Receptor-like Antibody Recognizes Major Histocompatibility Complex-bound Peptide

Human Cerberus prevents nodal-receptor binding, inhibits nodal signaling, and suppresses nodal-mediated phenotypes

Kinetics of quinine-deuterohemin binding

New Ligand Binding Function of Human Cerberus and Role of Proteolytic Processing in Regulating Ligand-Receptor Interactions and Antagonist Activity.

Orientation of OmpR monomers within an OmpR:DNA complex determined by DNA affinity cleaving 1 1Edited by K. Yamamoto

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes.

Specificity and Structure of a High Affinity Activin Receptor-like Kinase 1 (ALK1) Signaling Complex

Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26

Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis

The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor

Transforming Growth Factor-β Family Ligands Can Function as Antagonists by Competing for Type II Receptor Binding.