Evidence map›Paper›PMID 30338221›Full record

ArticleFEBS open bio2018

Oxidation-resistant and thermostable forms of alpha-1 antitrypsin from

Wei Zhu, Lanfen Li, Mingjing Deng, Bo Wang, Mengfei Li, Guofang Ding, Zuisu Yang, Dan Medynski, Xiaotao Lin, Ying Ouyang and 3 more

Abstract read
In one paragraph

Article in FEBS open bio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. EvoMut: A computational framework for engineering oxidative stability in proteins.Protein science : a publication of the Protein Society · 2026
    Article
  2. Nebulizers effectiveness on pulmonary delivery of alpha-1 antitrypsin.Drug delivery and translational research · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Engineering the serpin αProtein science : a publication of the Protein Society · 2020
    Review
  9. Dysregulation of the glutaredoxin/American journal of physiology. Cell physiology · 2020
    Article
  10. Article
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

13 authors.

Wei ZhuKey Laboratory for Microorganisms and Biotransformation College of Life Science South-Central University for Nationalities Wuhan China.
Lanfen LiState Key Laboratory of Protein and Plant Gene Research School of Life Sciences Peking University Beijing China.
Mingjing DengState Key Laboratory of Protein and Plant Gene Research School of Life Sciences Peking University Beijing China.
Bo WangState Key Laboratory of Protein and Plant Gene Research School of Life Sciences Peking University Beijing China.
Mengfei LiKey Laboratory for Microorganisms and Biotransformation College of Life Science South-Central University for Nationalities Wuhan China.
Guofang DingKey Engineering Research Centers of Marine Organisms Medical Products Food and Medicine School of Zhejiang Ocean University Zhoushan China.
Zuisu YangKey Engineering Research Centers of Marine Organisms Medical Products Food and Medicine School of Zhejiang Ocean University Zhoushan China.
Dan MedynskiCardinal Intellectual Property LLC Oakland CA USA.
Xiaotao LinShenzhen YHLO Biotech Co., Ltd. Shenzhen China.
Ying OuyangWuxi Biortus Biosciences Co., Ltd. Jiangyin China.
Jirui LinSchool of Software Huazhong University of Science and Technology Wuhan China.
Luyuan LiState Key Laboratory of Medicinal Chemical Biology Nankai University College of Pharmacy Tianjin China.
Xinli LinKey Laboratory for Microorganisms and Biotransformation College of Life Science South-Central University for Nationalities Wuhan China.ORCID 0000-0002-5420-7264

Funding

Recombinant alpha1-Antitrypsin TherapeuticsR43HL102979 · NHLBI · GENECOPOEIA, INC. · PI LIN, XINLI HENRY · 2010 to 2010
$107k
NHLBI NIH HHS R43 HL102979
6 · The paper itself

Abstract

Native α1-antitrypsin (AAT) is a 52-kDa glycoprotein that acts as an antiprotease and is the physiological inhibitor of neutrophil serine proteases. The main function of AAT is to protect the lung from proteolytic damage induced by inflammation. AAT deficiency (AATD) is a codominant autosomal disorder caused by pathogenic mutations in SERPINA1 gene, leading to reduced levels of serum AAT. The deficiency is known to increase the risk of pulmonary emphysema and chronic obstructive pulmonary disease as a consequence of proteolytic imbalance induced by inflammation, associated in many instances with cigarette smoking and other environmental hazards. Currently, the available therapy for lung disease associated with AATD is serum purified human AAT injected into patients on a weekly basis. It would be advantageous to replace serum-derived AAT with a recombinant version which is stable and resistant to oxidation. We have expressed AAT in

Indexed as

Escherichia coli inclusion body refoldingmutant alpha‐1 antitrypsinprotease inhibitorprotein therapeuticrecombinant protein

Identifiers

PMID30338221
PMCPMC6168689

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.