Evidence map›Paper›PMID 32794130›Full record

ArticlePharmaceutical research2020

Evaluation of Predictors of Protein Relative Stability Obtained by Solid-State Hydrogen/Deuterium Exchange Monitored by FTIR.

Rui Fang, Wasfy Obeidat, Michael J Pikal, Robin H Bogner

Erratum issuedAbstract read
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In one paragraph

Article in Pharmaceutical research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025
    Review
  2. Article
  3. Article
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Rui FangUniversity of Connecticut, Storrs, Connecticut, USA.
Wasfy ObeidatUniversity of Connecticut, Storrs, Connecticut, USA.
Michael J PikalUniversity of Connecticut, Storrs, Connecticut, USA.
Robin H BognerUniversity of Connecticut, Storrs, Connecticut, USA. Robin.bogner@uconn.edu.ORCID http://orcid.org/0000-0003-3710-9889

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeHydrogen/deuterium (H/D) exchange over a range of temperatures suggests a protein structural/mobility transition in the solid state below the system glass transition temperature (T

methodsSolid-state H/D exchange was monitored by FTIR spectroscopy to study the extent of exchange and the apparent transition temperature in both pure recombinant human serum albumin (rHSA) and rHSA formulated with sucrose or trehalose. H/D exchange of freeze-dried formulations at 11% RH and temperatures from 30 to 80°C was monitored. Protein stability against aggregation at 40°C/11% RH for 6 months was assessed by size exclusion chromatography (SEC).

resultsBoth sucrose and trehalose showed equivalent protection of protein secondary structure by FTIR. The rHSA:sucrose formulation showed superior long-term stability at 40°C by SEC over the trehalose formulation, but the apparent T

conclusionsWhile apparent T

Indexed as

Protein StabilityChemistry, PhysicalDeuteriumFreeze DryingHumansHydrogenProtein Structure, SecondaryRecombinant ProteinsSerum Albumin, HumanSpectroscopy, Fourier Transform InfraredSucroseTransition TemperatureTrehaloseDeuteriumHydrogenRecombinant ProteinsSerum Albumin, HumanSucroseTrehaloseFreeze-dryingFTIRprotein internal dynamicsprotein stabilitysolid-state H/D exchange

Identifiers

PMID32794130

What OpenQuestion holds

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Registered trials

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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.