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Kemp elimination catalysts by computational enzyme design
scientific article
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instance of
scholarly article
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title
Kemp elimination catalysts by computational enzyme design
(English)
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author
Daniela Röthlisberger
series ordinal
1
object named as
Daniela Röthlisberger
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David Baker
object named as
David Baker
series ordinal
14
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Kendall Houk
series ordinal
12
object named as
Kendall N Houk
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author name string
Daniela Röthlisberger
series ordinal
1
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Olga Khersonsky
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2
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Andrew M Wollacott
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3
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Lin Jiang
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4
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Jason DeChancie
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5
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Jamie Betker
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6
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Jasmine L Gallaher
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7
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Eric A Althoff
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8
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Alexandre Zanghellini
series ordinal
9
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Orly Dym
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10
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Shira Albeck
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11
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Dan S Tawfik
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13
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language of work or name
English
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publication date
8 May 2008
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published in
Nature
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volume
453
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page(s)
190-5
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issue
7192
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cites work
Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
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A proficient enzyme
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Enzyme-like proteins by computational design
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De novo design of catalytic proteins
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Crossref
reference URL
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7 January 2021
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inferred from DOI database lookup
New algorithms and an in silico benchmark for computational enzyme design
1 reference
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Crossref
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7 January 2021
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inferred from DOI database lookup
Physical organic chemistry of benzisoxazoles. II. Linearity of the Broensted free energy relation for the base-catalyzed decomposition of benzisoxazoles
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Crossref
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Nonspecific medium effects versus specific group positioning in the antibody and albumin catalysis of the base-promoted ring-opening reactions of benzisoxazoles
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Structural origins of efficient proton abstraction from carbon by a catalytic antibody
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Density-functional exchange-energy approximation with correct asymptotic behavior
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7 January 2021
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inferred from DOI database lookup
Analysis of anisotropic side-chain packing in proteins and application to high-resolution structure prediction.
1 reference
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Crossref
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7 January 2021
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inferred from DOI database lookup
Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
1 reference
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7 January 2021
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ROSETTALIGAND: protein-small molecule docking with full side-chain flexibility.
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Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design
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7 January 2021
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Selection and evolution of enzymes from a partially randomized non-catalytic scaffold
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Turnover-based in vitro selection and evolution of biocatalysts from a fully synthetic antibody library.
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Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity.
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Large rate accelerations in antibody catalysis by strategic use of haptenic charge
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Off-the-shelf proteins that rival tailor-made antibodies as catalysts.
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De novo computational design of retro-aldol enzymes
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7 January 2021
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Hypermutagenic PCR involving all four transitions and a sizeable proportion of transversions.
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High efficiency family shuffling based on multi-step PCR and in vivo DNA recombination in yeast: statistical and functional analysis of a combinatorial library between human cytochrome P450 1A1 and 1A2
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Incorporating Synthetic Oligonucleotides via Gene Reassembly (ISOR): a versatile tool for generating targeted libraries
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A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins
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7 January 2021
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inferred from DOI database lookup
Rapid and efficient site-specific mutagenesis without phenotypic selection
1 reference
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Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
Protein production by auto-induction in high density shaking cultures
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Crossref
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7 January 2021
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inferred from DOI database lookup
How to measure and predict the molar absorption coefficient of a protein
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Crossref
reference URL
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7 January 2021
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Identifiers
DOI
10.1038/NATURE06879
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
31815
Dimensions Publication ID
1027980204
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OpenCitations bibliographic resource ID
31815
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
31815
PubMed ID
18354394
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
31815
ResearchGate publication ID
5498861
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Springer Nature article ID
10.1038/nature06879
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