Evidence map›Paper›PMID 21513457›Full record

ReviewAnnual review of biochemistry2011

Biological phosphoryl-transfer reactions: understanding mechanism and catalysis.

Jonathan K Lassila, Jesse G Zalatan, Daniel Herschlag

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 196 papers.

0numbers the graph read from it
0cells of the map it votes in
196citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

196 citing papers in PubMed.

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  19. The journal of physical chemistry. C, Nanomaterials and interfaces · 2025
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136 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Jonathan K LassilaDepartment of Biochemistry, Stanford University, Stanford, California 94305, USA. lassila@stanford.edu
Jesse G Zalatan
Daniel Herschlag

Funding

Study of Nonenzymatic and Enzymatic Phosphoryl TransferR01GM064798 · NIGMS · STANFORD UNIVERSITY · PI Polly Morrell Fordyce, DANIEL HERSCHLAG · 2002 to 2026
$5.9M
Catalytic specificity of zinc phosphate esterases investigated by evolutionF32GM080865 · NIGMS · STANFORD UNIVERSITY · PI LASSILA, JONATHAN K · 2007 to 2009
$142k
NIGMS NIH HHS F32 GM080865NIGMS NIH HHS GM080865NIGMS NIH HHS GM64798NIGMS NIH HHS R01 GM064798
6 · The paper itself

Abstract

Phosphoryl-transfer reactions are central to biology. These reactions also have some of the slowest nonenzymatic rates and thus require enormous rate accelerations from biological catalysts. Despite the central importance of phosphoryl transfer and the fascinating catalytic challenges it presents, substantial confusion persists about the properties of these reactions. This confusion exists despite decades of research on the chemical mechanisms underlying these reactions. Here we review phosphoryl-transfer reactions with the goal of providing the reader with the conceptual and experimental background to understand this body of work, to evaluate new results and proposals, and to apply this understanding to enzymes. We describe likely resolutions to some controversies, while emphasizing the limits of our current approaches and understanding. We apply this understanding to enzyme-catalyzed phosphoryl transfer and provide illustrative examples of how this mechanistic background can guide and deepen our understanding of enzymes and their mechanisms of action. Finally, we present important future challenges for this field.

Indexed as

CatalysisHydrolysisIsotopesKineticsMolecular StructurePhosphatesPhosphorylationras ProteinsStatic ElectricityIsotopesPhosphatesras Proteins

Identifiers

PMID21513457
PMCPMC3418923

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.