(Q35073088)

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Analysis of high affinity self-association by fluorescence optical sedimentation velocity analytical ultracentrifugation of labeled proteins: opportunities and limitations

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Analysis of high affinity self-association by fluorescence optical sedimentation velocity analytical ultracentrifugation of labeled proteins: opportunities and limitations (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

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Peter Schuck

5

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author name string

Huaying Zhao

1

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Suvendu Lomash

2

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Carla Glasser

3

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Europe PubMed Central

PubMed publication ID

6 August 2017

Mark L Mayer

4

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Europe PubMed Central

PubMed publication ID

6 August 2017

language of work or name

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publication date

17 December 2013

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Europe PubMed Central

PubMed publication ID

6 August 2017

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Europe PubMed Central

PubMed publication ID

6 August 2017

8

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Europe PubMed Central

PubMed publication ID

6 August 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

e83439

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

copyright license

Creative Commons CC0 License

17 December 2013

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted, dedicated to the public domain by copyright holder

0 references

Tools for the quantitative analysis of sedimentation boundaries detected by fluorescence optical analytical ultracentrifugation

1 reference

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Analytical Ultracentrifugation as a Tool for Studying Protein Interactions

1 reference

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8 July 2018

Are fluorescence-detected sedimentation velocity data reliable?

1 reference

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Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation

1 reference

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

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1 reference

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Sedimentation patterns of rapidly reversible protein interactions.

1 reference

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Assembly, loading, and alignment of an analytical ultracentrifuge sample cell

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The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugation

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The extraordinary ligand binding properties of human serum albumin

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On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation

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Fluorescence-detected sedimentation in dilute and highly concentrated solutions

1 reference

https://pubmed.ncbi.nlm.nih.gov/24358283

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

[Applications and future perspectives of analytical ultracentrifugation]

1 reference

https://pubmed.ncbi.nlm.nih.gov/24358283

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains

1 reference

https://pubmed.ncbi.nlm.nih.gov/24358283

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1371/JOURNAL.PONE.0083439

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

2013PLoSO...883439Z

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ResearchGate publication ID

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