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Rational design of a tripartite fusion protein of heparinase I enables one-step affinity purification and real-time activity detection

https://doi.org/10.1016/j.jbiotec.2012.09.016

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0290(19991005)65:1<17::aid-bit3>3.0.co;2-yopenalex-snapshot

Immobilization of recombinant heparinase I fused to cellulose-binding domain

inferredcites →https://doi.org/10.1002/bit.10331openalex-snapshot

Integrated bioprocessing in Saccharomyces cerevisiae using green fluorescent protein as a fusion partner

inferredcites →https://doi.org/10.1002/bit.21396openalex-snapshot

Strategy for selecting and characterizing linker peptides for CBM9‐tagged fusion proteins expressed in Escherichia coli

inferredcites →https://doi.org/10.1002/bit.23144openalex-snapshot

Biochemical analysis and kinetic modeling of the thermal inactivation of MBP‐fused heparinase I: Implications for a comprehensive thermostabilization strategy

inferredcites →https://doi.org/10.1002/prot.20244openalex-snapshot

Conformations of variably linked chimeric proteins evaluated by synchrotron X‐ray small‐angle scattering

inferredcites →https://doi.org/10.1006/abio.1997.2181openalex-snapshot

Engineering of Functional Chimeric Protein G–VargulaLuciferase

inferredcites →https://doi.org/10.1006/abio.1999.4235openalex-snapshot

The Length of Polypeptide Linker Affects the Stability of Green Fluorescent Protein Fusion Proteins

inferredcites →https://doi.org/10.1007/s00216-008-2412-2openalex-snapshot

Advances in the separation, sensitive detection, and characterization of heparin and heparan sulfate

inferredcites →https://doi.org/10.1007/s00253-008-1468-4openalex-snapshot

Bifunctional enhancement of a β-glucanase-xylanase fusion enzyme by optimization of peptide linkers

inferredcites →https://doi.org/10.1007/s00253-011-3641-4openalex-snapshot

Engineering of routes to heparin and related polysaccharides

inferredcites →https://doi.org/10.1007/s00253-012-3967-6openalex-snapshot

Microbial heparin/heparan sulphate lyases: potential and applications

inferredcites →https://doi.org/10.1007/s00253-012-4145-6openalex-snapshot

Combination of site-directed mutagenesis and calcium ion addition for enhanced production of thermostable MBP-fused heparinase I in recombinant Escherichia coli

inferredcites →https://doi.org/10.1007/s002539900286openalex-snapshot

A green fluorescent protein fusion strategy for monitoring the expression, cellular location, and separation of biologically active organophosphorus hydrolase

inferredcites →https://doi.org/10.1007/s11095-008-9767-0openalex-snapshot

Insertion of the Designed Helical Linker Led to Increased Expression of Tf-Based Fusion Proteins

inferredcites →https://doi.org/10.1016/0022-2836(90)90085-zopenalex-snapshot

An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion

inferredcites →https://doi.org/10.1016/j.bbrc.2005.08.095openalex-snapshot

Production of Hev b5 as a fluorescent biotin-binding tripartite fusion protein in insect cells

inferredcites →https://doi.org/10.1016/j.bej.2004.12.001openalex-snapshot

Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein

inferredcites →https://doi.org/10.1016/j.bej.2006.11.020openalex-snapshot

Production of MBP–HepA fusion protein in recombinant Escherichia coli by optimization of culture medium

inferredcites →https://doi.org/10.1016/j.bej.2009.05.007openalex-snapshot

Characteristics of low molecular weight heparin production by an ultrafiltration membrane bioreactor using maltose binding protein fused heparinase I

inferredcites →https://doi.org/10.1016/j.biocel.2007.04.028openalex-snapshot

Role of the linker between the N- and C-terminal domains in the stability and folding of rabbit muscle creatine kinase

inferredcites →https://doi.org/10.1016/j.jbiosc.2009.08.303openalex-snapshot

Design of intelligent heparinase by fusion with maltose binding protein and fluorescent proteins

inferredcites →https://doi.org/10.1016/j.pep.2008.04.013openalex-snapshot

Increasing the homogeneity, stability and activity of human serum albumin and interferon-α2b fusion protein by linker engineering

inferredcites →https://doi.org/10.1016/s0021-9258(18)34377-1openalex-snapshot

Differential anticoagulant activity of heparin fragments prepared using microbial heparinase.

inferredcites →https://doi.org/10.1016/s0021-9258(18)35772-7openalex-snapshot

Purification and characterization of heparin lyases from Flavobacterium heparinum.

inferredcites →https://doi.org/10.1016/s0021-9258(18)89671-5openalex-snapshot

Purification and characterization of heparinase from Flavobacterium heparinum.

inferredcites →https://doi.org/10.1016/s0167-4838(99)00154-5openalex-snapshot

Engineering and biochemical characterization of the rat microsomal cytochrome P4501A1 fused to ferredoxin and ferredoxin–NADP+ reductase from plant chloroplasts

inferredcites →https://doi.org/10.1016/s1004-9541(07)60044-5openalex-snapshot

Soluble Expression and Rapid Quantification of GFP-hepA Fusion Protein in Recombinant Escherichia coli

inferredcites →https://doi.org/10.1016/s1367-5931(99)00046-0openalex-snapshot

Role of linkers in communication between protein modules

inferredcites →https://doi.org/10.1021/bi00462a026openalex-snapshot

Examination of the substrate specificity of heparin and heparan sulfate lyases

inferredcites →https://doi.org/10.1021/bi700164qopenalex-snapshot

Molecular Characterization of Specifically Active Recombinant Fused Enzymes Consisting of CYP3A4, NADPH-Cytochrome P450 Oxidoreductase, and Cytochromeb5

inferredcites →https://doi.org/10.1038/10904openalex-snapshot

Rapid protein-folding assay using green fluorescent protein

inferredcites →https://doi.org/10.1073/pnas.1103659108openalex-snapshot

Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP + -oxidoreductase (FNR) enzymes in vitro

inferredcites →https://doi.org/10.1073/pnas.84.24.8898openalex-snapshot

Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.

inferredcites →https://doi.org/10.1073/pnas.85.16.5879openalex-snapshot

Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli.

inferredcites →https://doi.org/10.1073/pnas.90.8.3660openalex-snapshot

Cloning and expression of heparinase I gene from Flavobacterium heparinum.

inferredcites →https://doi.org/10.1074/jbc.271.37.22462openalex-snapshot

Putidaredoxin Reductase-Putidaredoxin-Cytochrome P450cam Triple Fusion Protein

inferredcites →https://doi.org/10.1074/jbc.272.28.17605openalex-snapshot

Two Modes of Ligand Binding in Maltose-binding Protein ofEscherichia coli

inferredcites →https://doi.org/10.1074/jbc.272.28.17610openalex-snapshot

Two Modes of Ligand Binding in Maltose-binding Protein ofEscherichia coli

inferredcites →https://doi.org/10.1074/jbc.272.28.17615openalex-snapshot

Two Modes of Ligand Binding in Maltose-binding Protein ofEscherichia coli

inferredcites →https://doi.org/10.1074/jbc.m109.025338openalex-snapshot

Structural Snapshots of Heparin Depolymerization by Heparin Lyase I

inferredcites →https://doi.org/10.1074/jbc.m109.090936openalex-snapshot

Flexibility between the Protease and Helicase Domains of the Dengue Virus NS3 Protein Conferred by the Linker Region and Its Functional Implications

inferredcites →https://doi.org/10.1093/protein/13.5.309openalex-snapshot

LINKER: a program to generate linker sequences for fusion proteins

inferredcites →https://doi.org/10.1093/protein/14.8.529openalex-snapshot

Design of the linkers which effectively separate domains of a bifunctional fusion protein

inferredcites →https://doi.org/10.1093/protein/15.11.871openalex-snapshot

An analysis of protein domain linkers: their classification and role in protein folding

inferredcites →https://doi.org/10.1111/j.1574-6968.2006.00367.xopenalex-snapshot

Construction and characterization of a bifunctional fusion enzyme ofBacillus-sourced β-glucanase and xylanase expressed inEscherichia coli

inferredcites →https://doi.org/10.1128/aem.01241-09openalex-snapshot

Effect of Linker Length and Dockerin Position on Conversion of a Thermobifida fusca Endoglucanase to the Cellulosomal Mode

inferredcites →https://doi.org/10.1529/biophysj.105.069443openalex-snapshot

A Salt-Bridge Motif Involved in Ligand Binding and Large-Scale Domain Motions of the Maltose-Binding Protein

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4654627openalex-extracted

inferred← citeshttps://doi.org/10.1002/bab.2642openalex-snapshot

Characterization of maltose‐binding protein–fused heparinases with enhanced thermostability by application of rigid and flexible linkers

inferred← citeshttps://doi.org/10.1002/biot.201700627openalex-snapshot

Design of Fusion Proteins for Efficient and Soluble Production of Immunogenic Ebola Virus Glycoprotein inEscherichia coli

inferred← citeshttps://doi.org/10.1007/s00203-022-03158-4openalex-snapshot

Expression and characterization of heparinase II with MBP tag from a novel strain, Raoultella NX-TZ-3-15

inferred← citeshttps://doi.org/10.1007/s00253-015-6985-3openalex-snapshot

Construction of a linker library with widely controllable flexibility for fusion protein design

inferred← citeshttps://doi.org/10.1016/j.bej.2024.109253openalex-snapshot

Engineering artificial fusion naringinase for enhancing naringenin biosynthesis

inferred← citeshttps://doi.org/10.1016/j.biochi.2022.03.011openalex-snapshot

Production, characteristics and applications of microbial heparinases

inferred← citeshttps://doi.org/10.1016/j.biotechadv.2022.108016openalex-snapshot

Design and biocatalytic applications of genetically fused multifunctional enzymes

inferred← citeshttps://doi.org/10.1016/j.cjche.2023.06.015openalex-snapshot

α-Synuclein: A fusion chaperone significantly boosting the enzymatic performance of PET hydrolase

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2015.11.002openalex-snapshot

A study on the effects of linker flexibility on acid phosphatase PhoC-GFP fusion protein using a novel linker library

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2020.109549openalex-snapshot

Engineering the heparin-binding pocket to enhance the catalytic efficiency of a thermostable heparinase III from Bacteroides thetaiotaomicron

inferred← citeshttps://doi.org/10.1016/j.fbio.2024.105651openalex-snapshot

Fusion of two chitinases from Vibrio harveyi to enhance enzyme stability and degradation efficiency on chitin and shrimp shell

inferred← citeshttps://doi.org/10.1016/j.psep.2025.106818openalex-snapshot

Construction of Yarrowia lipolytica for degradation of low-density polyethylene

inferred← citeshttps://doi.org/10.1021/acscatal.4c05616openalex-snapshot

Keeping the Distance: Activity Control in Solid-Supported Sucrose Phosphorylase by a Rigid α-Helical Linker of Tunable Spacer Length

inferred← citeshttps://doi.org/10.1080/07388551.2017.1303803openalex-snapshot

Strategies and perspectives of assembling multi-enzyme systems

inferred← citeshttps://doi.org/10.1186/s12934-020-01501-2openalex-snapshot

Construction and characterization of a novel glucose dehydrogenase-leucine dehydrogenase fusion enzyme for the biosynthesis of l-tert-leucine

inferred← citeshttps://doi.org/10.26599/fshw.2024.9250134openalex-snapshot

Rational protein engineering of thermostable heparinase Ⅰ from Bacteroides thetaiotaomicron for highly efficient heparin degradation

inferred← citeshttps://doi.org/10.6084/m9.figshare.13534673openalex-snapshot

Additional file 1 of Construction and characterization of a novel glucose dehydrogenase-leucine dehydrogenase fusion enzyme for the biosynthesis of l-tert-leucine

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