Folding kinetic pathway of phosphofructokinase-2 fromEscherichia coli: A homodimeric enzyme with a complex domain organization

28 May 2018

reason for preferred rank

title

Folding kinetic pathway of phosphofructokinase-2 fromEscherichia coli: A homodimeric enzyme with a complex domain organization (English)

1 reference

https://api.crossref.org/works/10.1016/J.FEBSLET.2011.05.041

3 December 2024

Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21627967

3 December 2024

1 reference

protein secondary structure

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21627967

3 December 2024

protein folding

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21627967

3 December 2024

2

Christian A. M. Wilson

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21627967

3 December 2024

author name string

Mauricio Baez

1

1 reference

28 May 2018

Jorge Babul

3

1 reference

28 May 2018

language of work or name

English

0 references

publication date

27 May 2011

1 reference

28 May 2018

full work available at URL

https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2011.05.041

1 reference

https://api.crossref.org/works/10.1016/J.FEBSLET.2011.05.041

https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2011.05.041

3 December 2024

1 reference

https://api.crossref.org/works/10.1016/J.FEBSLET.2011.05.041

http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2011.05.041/fullpdf

3 December 2024

1 reference

https://api.crossref.org/works/10.1016/J.FEBSLET.2011.05.041

3 December 2024

1 reference

28 May 2018

volume

585

1 reference

28 May 2018

issue

14

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28 May 2018

page(s)

2158-2164

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28 May 2018

Ribokinase family evolution and the role of conserved residues at the active site of the PfkB subfamily representative, Pfk-2 from Escherichia coli

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Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures

21 January 2018

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Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition

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Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability

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Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains

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Pathways of protein folding

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The linkage between protein folding and functional cooperativity: two sides of the same coin?

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Multiple routes and structural heterogeneity in protein folding

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Conformational stability and folding mechanisms of dimeric proteins

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Protein topology determines binding mechanism

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Principles of protein-protein interactions

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Structural motifs at protein-protein interfaces: protein cores versus two-state and three-state model complexes

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Hydrophobic folding units at protein-protein interfaces: implications to protein folding and to protein-protein association

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Folding and association of proteins

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Equilibrium dissociation and unfolding of the Arc repressor dimer

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The folding cooperativity of a protein is controlled by its chain topology

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Sequential vs. parallel protein-folding mechanisms: experimental tests for complex folding reactions

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VMD: visual molecular dynamics

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P22 Arc repressor: folding kinetics of a single-domain, dimeric protein

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