CoChat
Sign Up
Cited by 290Protease and Inhibitor MechanismsEnzyme Production and CharacterizationEnzyme Structure and Function

The DOI matches its Crossref record; 75 of the 77 references it cites were found in a registry or an index.

Research Applications of Proteolytic Enzymes in Molecular Biology

Open access
Mótyán, János, Tóth, Ferenc, Tőzsér, József·2013·Biomolecules
DOI 10.3390/biom3040923PMC PMC4030975
Open this paper in CoChat — free accountOpen PDF

Abstract

Proteolytic enzymes (also termed peptidases, proteases and proteinases) are capable of hydrolyzing peptide bonds in proteins. They can be found in all living organisms, from viruses to animals and humans. Proteolytic enzymes have great medical and pharmaceutical importance due to their key role in biological processes and in the life-cycle of many pathogens. Proteases are extensively applied enzymes in several sectors of industry and biotechnology, furthermore, numerous research applications require their use, including production of Klenow fragments, peptide synthesis, digestion of unwanted proteins during nucleic acid purification, cell culturing and tissue dissociation, preparation of recombinant antibody fragments for research, diagnostics and therapy, exploration of the structure-function relationships by structural studies, removal of affinity tags from fusion proteins in recombinant protein techniques, peptide sequencing and proteolytic digestion of proteins in proteomics. The aim of this paper is to review the molecular biological aspects of proteolytic enzymes and summarize their applications in the life sciences.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/biom3040923

Cites

75 of 75 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Action of aminopeptidases and carboxypeptidases removing the terminal amino acid residues as well as endopeptidases on a polypeptide substrate (having n residues). Red arrows show the peptide bonds to be cleaved.
Figure 1 Action of aminopeptidases and carboxypeptidases removing the terminal amino acid residues as well as endopeptidases on a polypeptide substrate (having n residues). Red arrows show the peptide bonds to be cleaved.CC BY · PubMed Central
Figure 2 Kinetically-controlled synthesis of Z-d-Leu-l-Leu-NH2 dipeptide. After the formation of enzyme-substrate complex (K1) a covalent enzyme-substrate intermediate is formed (K2). The intermediate is subjected to the attack from H2O or other nucleophiles (Nu). KH is the equilibrium constant of hydrolysis, KT is the equilibrium constant of the transferase reaction.
Figure 2 Kinetically-controlled synthesis of Z-d-Leu-l-Leu-NH2 dipeptide. After the formation of enzyme-substrate complex (K1) a covalent enzyme-substrate intermediate is formed (K2). The intermediate is subjected to the attack from H2O or other nucleophiles (Nu). KH is the equilibrium constant of hydrolysis, KT is the equilibrium constant of the transferase reaction.CC BY · PubMed Central
Figure 3 Structure of IgG antibody molecules (A) and fragments released after proteolytic digestion using papain (B), pepsin (C) or ficin (D).
Figure 3 Structure of IgG antibody molecules (A) and fragments released after proteolytic digestion using papain (B), pepsin (C) or ficin (D).CC BY · PubMed Central
Figure 4 Steps of proteomic analysis using mass-spectrometry after separation and in-gel digestion of proteins of interest.
Figure 4 Steps of proteomic analysis using mass-spectrometry after separation and in-gel digestion of proteins of interest.CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 77 references

Research works printed but not linked: 4

  1. Rani, 2012, Review on latest overview of proteases, Int. J. Curr. Life Sci., 2, 12
  2. Bhalla, 1999, Thermophilic bacterial proteases, J. Punjab Acad. Sci., 1, 77
  3. Ragnurrson, U. (, 1985). Use of Proteolytic Enzymes for the Synthesis of Fragments of Mouse Epidermal Growth Factor. Proceedings of Peptides 1984, Almquist, Stockholm.
  4. Adamczak, 2004, Enzyme for efficient biocatalysis, Food Technol. Biotechnol., 42, 251

Cited by

Sorted by citations

Items 101–200 of 290

Related

See all

Metadata

Authors
Mótyán, J., Tóth, F., & Tőzsér, J.
Affiliations
University of Debrecen (HU)
Corresponding author
Tőzsér, József
ORCID
Venue
Biomolecules
Publisher
MDPI AG
Published
2013-11-08
Volume
3
Issue
4
Pages
923-942
ISSN
2218-273X (ISSN-L)
DOI
10.3390/biom3040923
PMC
PMC4030975
OpenAlex
W2130109271
Cited by
267
References
77
Citations by year
2026: 14 · 2025: 24 · 2024: 34 · 2023: 38 · 2022: 29 · 2021: 32 · 2020: 26 · 2019: 31 · 2018: 11 · 2017: 7 · 2016: 9 · 2015: 5 · 2014: 5
FWCI
2.23
Type
journal article
Language
en
Open access
Licence
Locations
  • Biomolecules (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
Funders
  • European Regional Development Fund
  • European Social Fund
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
proteolytic enzymes, Klenow fragment, peptide synthesis, nucleic acid purification, tissue dissociation, recombinant antibody fragments, proteomics, peptide sequencing, structure-function relationship, protease inhibitors

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review