Evidence map›Paper›PMID 31012517›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019

Substitution of an Internal Disulfide Bridge with a Diselenide Enhances both Foldability and Stability of Human Insulin.

Orit Weil-Ktorza, Nischay Rege, Shifra Lansky, Deborah E Shalev, Gil Shoham, Michael A Weiss, Norman Metanis

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Effects of Selenocysteine Substitution on the Cyclotide Kalata B2.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Semisynthesis of A6-A11 lactam insulin.Journal of peptide science : an official publication of the European Peptide Society · 2024
    Article
  12. Article
  13. Selenium in Peptide Chemistry.Molecules (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

7 authors.

Orit Weil-KtorzaThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra, Givat Ram, Jerusalem, 91904, Israel.
Nischay RegeDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, 44106, USA.
Shifra LanskyThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra, Givat Ram, Jerusalem, 91904, Israel.
Deborah E ShalevWolfson Center for Applied Structural Biology, The Hebrew University of Jerusalem, Edmond J. Safra, Givat Ram, Jerusalem, 91904, Israel.
Gil ShohamThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra, Givat Ram, Jerusalem, 91904, Israel.
Michael A WeissDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, 44106, USA.
Norman MetanisThe Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra, Givat Ram, Jerusalem, 91904, Israel.ORCID http://orcid.org/0000-0002-6373-9318

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007250 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI HUANG, ALEX YEE-CHEN · 1985 to 2023
$33.4M
Development and characterization of ultra-stable insulin analogs for novel therapeutic useF30DK112644 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI REGE, NISCHAY KIRAN · 2016 to 2020
$179k
Foundation for the National Institutes of Health NIH R01 DK04949Israel Cancer Research Fund Acceleration GrantIsrael Science Foundation 1905/15Israel Science Foundation 783/18Ministry of Science,Technology and space (MOST) 3-12484/15NIDDK NIH HHS F30 DK112644NIGMS NIH HHS T32 GM007250Predoctoral Fellow of the Medical Scientist Training Program at CWRU NIH 5T32GM007250-38 and NIH Fellowship 1F30DK112644
6 · The paper itself

Abstract

Insulin analogues, mainstays in the modern treatment of diabetes mellitus, exemplify the utility of protein engineering in molecular pharmacology. Whereas chemical syntheses of the individual A and B chains were accomplished in the early 1960s, their combination to form native insulin remains inefficient because of competing disulfide pairing and aggregation. To overcome these limitations, we envisioned an alternative approach: pairwise substitution of cysteine residues with selenocysteine (Sec, U). To this end, Cys

Indexed as

Crystallography, X-RayCysteineDisulfidesHumansInsulinProtein BindingProtein FoldingProtein StabilityProtein Structure, TertiaryReceptor, InsulinRecombinant ProteinsSeleniumSelenocysteineThermodynamicsCysteineDisulfidesInsulinReceptor, InsulinRecombinant ProteinsSeleniumSelenocysteinechemical protein synthesisinsulinoxidative protein foldingprotein engineeringprotein modificationsselenocysteine

Identifiers

PMID31012517
PMCPMC6861001

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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.