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Tryptophan tags and de novo designed complementary affinity ligands for the expression and purification of recombinant proteins

https://doi.org/10.1016/j.chroma.2016.10.017

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What this work says

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

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Single‐step recovery and solid‐phase refolding of inclusion body proteins using a polycationic purification tag

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Rapid Matrix‐Assisted Refolding of Histidine‐Tagged Proteins

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A Tailor‐Made “Tag–Receptor” Affinity Pair for the Purification of Fusion Proteins

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Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems

inferredcites →https://doi.org/10.1007/s10529-008-9696-3openalex-snapshot

Influence of tryptophan tags on the purification of cutinase, secreted by a recombinant Saccharomyces cerevisiae, using cationic expanded bed adsorption and hydrophobic interaction chromatography

inferredcites →https://doi.org/10.1007/s10822-013-9703-1openalex-snapshot

Structural evaluation of an alternative Protein A biomimetic ligand for antibody purification

inferredcites →https://doi.org/10.1016/j.biotechadv.2009.01.008openalex-snapshot

Production of recombinant proteins by microbes and higher organisms

inferredcites →https://doi.org/10.1016/j.biotechadv.2013.12.001openalex-snapshot

Challenges and opportunities in the purification of recombinant tagged proteins

inferredcites →https://doi.org/10.1016/j.chroma.2004.11.102openalex-snapshot

An artificial protein L for the purification of immunoglobulins and Fab fragments by affinity chromatography

inferredcites →https://doi.org/10.1016/j.chroma.2012.04.071openalex-snapshot

Understanding the molecular recognition between antibody fragments and protein A biomimetic ligand

inferredcites →https://doi.org/10.1016/j.chroma.2015.09.036openalex-snapshot

Mild and cost-effective green fluorescent protein purification employing small synthetic ligands

inferredcites →https://doi.org/10.1016/j.chroma.2016.02.026openalex-snapshot

Small synthetic ligands for the enrichment of viral particles pseudotyped with amphotropic murine leukemia virus envelope

inferredcites →https://doi.org/10.1016/j.chroma.2016.06.032openalex-snapshot

Mimicking nature: Phosphopeptide enrichment using combinatorial libraries of affinity ligands

inferredcites →https://doi.org/10.1016/j.jchromb.2009.03.010openalex-snapshot

Affinity ligands for immunoglobulins based on the multicomponent Ugi reaction

inferredcites →https://doi.org/10.1016/j.pep.2015.11.021openalex-snapshot

Npro fusion technology: On-column complementation to improve efficiency in biopharmaceutical production

inferredcites →https://doi.org/10.1016/j.tibtech.2010.11.003openalex-snapshot

Decorating microbes: surface display of proteins on Escherichia coli

inferredcites →https://doi.org/10.1016/j.tibtech.2011.09.003openalex-snapshot

Bacterial inclusion bodies: making gold from waste

inferredcites →https://doi.org/10.1016/s0076-6879(09)63017-2openalex-snapshot

Chapter 17 Refolding Solubilized Inclusion Body Proteins

inferredcites →https://doi.org/10.1016/s0076-6879(09)63027-5openalex-snapshot

Chapter 27 Immobilized-Metal Affinity Chromatography (IMAC)

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Role of Arginine in the Stabilization of Proteins against Aggregation

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Chromophore Formation in Green Fluorescent Protein

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Peptide fusion tags with tryptophan and charged residues for control of protein partitioning in PEG–potassium phosphate aqueous two-phase systems

inferredcites →https://doi.org/10.1038/nmeth0106-55openalex-snapshot

Strategies for protein coexpression in Escherichia coli

inferredcites →https://doi.org/10.1080/01496395.2010.507447openalex-snapshot

Comparison of Fluorescence Labelling Techniques for the Selection of Affinity Ligands from Solid-Phase Combinatorial Libraries

inferredcites →https://doi.org/10.1186/1472-6750-12-1openalex-snapshot

Single/low-copy integration of transgenes in Caenorhabditis elegans using an ultraviolet trimethylpsoralen method

inferredcites →https://doi.org/10.1186/1472-6750-12-65openalex-snapshot

Short-chain fluorescent tryptophan tags for on-line detection of functional recombinant proteins

inferredcites →https://doi.org/10.1263/jbb.99.303openalex-snapshot

Solubilization and refolding of bacterial inclusion body proteins

What points at this work

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

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De Novo Design Protein Receptors for Mbp and Gst Tags

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New multimodal stationary phases prepared by Ugi multicomponent approach

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Affinity Tags in Protein Purification and Peptide Enrichment: An Overview

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Biomimetic Affinity Ligands for Protein Purification

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Affinity-triggered hydrogels: Developments and prospects in biomaterials science

inferred← citeshttps://doi.org/10.1016/j.chroma.2018.01.009openalex-snapshot

Structure-based design and application of a nucleotide coenzyme mimetic ligand: Application to the affinity purification of nucleotide dependent enzymes

inferred← citeshttps://doi.org/10.1016/j.chroma.2020.460871openalex-snapshot

Rational design of affinity ligands for bioseparation

inferred← citeshttps://doi.org/10.1016/j.jare.2021.06.010openalex-snapshot

Tag-mediated single-step purification and immobilization of recombinant proteins toward protein-engineered advanced materials

inferred← citeshttps://doi.org/10.1021/acscombsci.8b00072openalex-snapshot

Materials Functionalization with Multicomponent Reactions: State of the Art

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Protein engineering of antibody fragments for pharmaceutical production

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