Different contribution of conserved amino acids to the global properties of triosephosphate isomerases-Reference-Cited by-同舟云学术

Different contribution of conserved amino acids to the global properties of triosephosphate isomerases

Published:2013-10-18 Issue:2 Volume:82 Page:323-335
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Aguirre Yolanda¹,Cabrera Nallely¹,Aguirre Beatriz¹,Pérez-Montfort Ruy¹,Hernandez-Santoyo Alejandra²,Reyes-Vivas Horacio³,Enríquez-Flores Sergio³,de Gómez-Puyou Marietta Tuena¹,Gómez-Puyou Armando¹,Sanchez-Ruiz Jose M.⁴,Costas Miguel⁵

Affiliation:

1. Departamento de Bioquímica y Biología Estructural; Instituto de Fisiología Celular; Universidad Nacional Autónoma de México; México D.F México

2. Instituto de Química; Universidad Nacional Autónoma de México; México D.F México

3. Laboratorio de Bioquímica-Genética; Torre de Investigación, Instituto Nacional de Pediatría, Secretaría de Salud; 04530, México, D.F México

4. Departamento de Química Física; Facultad de Ciencias, Universidad de Granada; Granada Spain

5. Laboratorio de Biofisicoquímica, Departamento de Fisicoquímica; Facultad de Química, Universidad Nacional Autónoma de México; México D.F México

Funder

Consejo Nacional de Ciencia y Tecnologia de Mexico

Dirección General de Asuntos del Personal Académico

Spanish Ministry of Science and Innovation

FEDER Funds

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.24398/fullpdf

Reference46 articles.

1. Context-dependent secondary structure formation of a designed protein sequence;Minor;Nature,1996

2. Evolutionary conserved pathways of energetic connectivity in protein families;Lockless;Science,1999

3. Identification of amino acids that account for long-range interactions in two triosephosphate isomerases from pathogenic trypanosomes;García-Torres;PLoS One,2011

4. The propagation of binding interactions to remote sites in proteins: and analysis of the monoclonal antibody D1.3 to lysozyme;Freire;Proc Natl Acad Sci USA,1999

5. Protein sectors: evolutionary units of three-dimensional structure;Halabi;Cell,2009

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