Evidence map›Paper›PMID 23377850›Full record

ArticleCurrent protocols in protein science2013

Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.

Huaying Zhao, Chad A Brautigam, Rodolfo Ghirlando, Peter Schuck

Abstract read
In one paragraph

Article in Current protocols in protein science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing 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

140 citing papers in PubMed.

  1. Review
  2. Structural and functional insights into the Rcs phosphorelay.bioRxiv : the preprint server for biology · 2026
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80 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

4 authors.

Huaying ZhaoDynamics of Macromolecular Assembly Section, Laboratory of Cellular Imaging and Macromolecular Biophysics, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, Maryland, USA.
Chad A Brautigam
Rodolfo Ghirlando
Peter Schuck

Funding

The flavin-centric metabolic lifestyle of Treponema pallidumR01AI056305 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI HENDRIXSON, DAVID R · 2003 to 2024
$9.6M
Dynamics of Protein Assemblies by Analytical UltracentrifugationZIAEB000051 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2025
$7.9M
STRUCTURAL STUDY OF RHO-GTPASE REGULATORS AND EFFECTORSR01GM056322 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 1997 to 2019
$5.7M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
INBORN ERRORS OF METABOLISM IN CELL CULTURER01DK026758 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI CHUANG, DAVID T · 1986 to 2010
$4.3M
Intramural NIH HHS ZIA EB000051NIAID NIH HHS AI056305NIAID NIH HHS R01 AI056305NIDDK NIH HHS DK026758NIDDK NIH HHS R01 DK026758NIGMS NIH HHS GM056322NIGMS NIH HHS R01 GM056322
6 · The paper itself

Abstract

Modern computational strategies have allowed for the direct modeling of the sedimentation process of heterogeneous mixtures, resulting in sedimentation velocity (SV) size-distribution analyses with significantly improved detection limits and strongly enhanced resolution. These advances have transformed the practice of SV, rendering it the primary method of choice for most existing applications of analytical ultracentrifugation (AUC), such as the study of protein self- and hetero-association, the study of membrane proteins, and applications in biotechnology. New global multisignal modeling and mass conservation approaches in SV and sedimentation equilibrium (SE), in conjunction with the effective-particle framework for interpreting the sedimentation boundary structure of interacting systems, as well as tools for explicit modeling of the reaction/diffusion/sedimentation equations to experimental data, have led to more robust and more powerful strategies for the study of reversible protein interactions and multiprotein complexes. Furthermore, modern mathematical modeling capabilities have allowed for a detailed description of many experimental aspects of the acquired data, thus enabling novel experimental opportunities, with important implications for both sample preparation and data acquisition. The goal of the current unit is to describe the current tools for the study of soluble proteins, detergent-solubilized membrane proteins and their interactions by SV and SE.

Indexed as

AlgorithmsBuffersData Interpretation, StatisticalMolecular WeightProtein BindingProteinsSoftwareSolutionsUltracentrifugationBuffersProteinsSolutions

Identifiers

PMID23377850
PMCPMC3652391

What OpenQuestion holds

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Read underepoch 390

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.