Increased Diels-Alderase activity through backbone remodeling guided by Foldit players (Q24625443)

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Language	Label	Description	Also known as
English	Increased Diels-Alderase activity through backbone remodeling guided by Foldit players	scientific article

Statements

instance of

scholarly article

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

title

Increased Diels-Alderase activity through backbone remodeling guided by Foldit players (English)

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

main subject

bioengineering

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biomedical engineering

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citizen science

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Foldit

1 reference

based on heuristic

inferred from title

author

Jacob B Bale

object named as

Jacob B Bale

series ordinal

3

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David Baker

object named as

David Baker

series ordinal

10

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Firas Khatib

series ordinal

5

object named as

Firas Khatib

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

Foldit Players

series ordinal

7

object named as

Foldit Players

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

Seth Cooper

series ordinal

4

object named as

Seth Cooper

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

Zoran B Popovic

series ordinal

9

object named as

Zoran Popovic

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

author name string

Christopher B Eiben

series ordinal

1

1 reference

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Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

Justin B Siegel

series ordinal

2

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stated in

Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

Betty W Shen

series ordinal

6

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stated in

Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

Barry L Stoddard

series ordinal

8

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

language of work or name

English

0 references

publication date

22 January 2012

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

published in

Nature Biotechnology

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stated in

Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

volume

30

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stated in

Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

issue

2

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stated in

Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

page(s)

190-192

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stated in

Europe PubMed Central

PubMed publication ID

22267011

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23 June 2017

describes a project that uses

crowdsourcing

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cites work

Predicting protein structures with a multiplayer online game

1 reference

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PubMed Central

reference URL

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7 April 2017

De novo computational design of retro-aldol enzymes

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7 April 2017

Crystal structure of a monomeric retroviral protease solved by protein folding game players

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7 April 2017

Computational Design of an Enzyme Catalyst for a Stereoselective Bimolecular Diels-Alder Reaction

1 reference

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PubMed Central

reference URL

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7 April 2017

Alteration of enzyme specificity by computational loop remodeling and design

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Kemp elimination catalysts by computational enzyme design

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7 April 2017

High-resolution design of a protein loop

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The helix turn helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Phasercrystallographic software

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The CCP4 suite: programs for protein crystallography

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Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris

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Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions

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Refinement of macromolecular structures by the maximum-likelihood method

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PROCHECK: a program to check the stereochemical quality of protein structures

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Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters

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Motif-directed flexible backbone design of functional interactions

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PubMed Central

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Catalytic versatility, stability, and evolution of the (betaalpha)8-barrel enzyme fold

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Design and evolution of new catalytic activity with an existing protein scaffold

1 reference

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Processing of X-ray diffraction data collected in oscillation mode

1 reference

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reference URL

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Identifiers

DOI

10.1038/NBT.2109

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

Dimensions Publication ID

1048326547

0 references

OpenCitations bibliographic resource ID

123963

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

123963

PMC publication ID

3566767

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

123963

PubMed publication ID

22267011

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22267011

retrieved

23 June 2017

ResearchGate publication ID

221768089

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