Ni(ii)-modified solid substrates as a platform to adsorb His-tag proteins-Reference-Cited by-同舟云学术

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Ni(ii)-modified solid substrates as a platform to adsorb His-tag proteins

Published:2013 Issue:38 Volume:1 Page:4921
ISSN:2050-750X
Container-title:Journal of Materials Chemistry B
language:en
Short-container-title:J. Mater. Chem. B

Author:

Valenti Laura E.,Martins Vitor L.,Herrera Elisa,Torresi Roberto M.,Giacomelli Carla E.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science,Biomedical Engineering,General Chemistry,General Medicine

Link

http://pubs.rsc.org/en/content/articlepdf/2013/TB/C3TB20769B

Reference49 articles.

1. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues

2. A Self-Assembled Monolayer for the Binding and Study of Histidine-Tagged Proteins by Surface Plasmon Resonance

3. XPS, TOF-SIMS, NEXAFS, and SPR Characterization of Nitrilotriacetic Acid-Terminated Self-Assembled Monolayers for Controllable Immobilization of Proteins

4. Self-Assembled Monolayers Containing Terminal Mono-, Bis-, and Tris-nitrilotriacetic Acid Groups: Characterization and Application

5. Surface-Specific Interaction of the Extracellular Domain of Protein L1 with Nitrilotriacetic Acid-Terminated Self-Assembled Monolayers

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5. Albumin biofunctionalization to minimize the Staphylococcus aureus adhesion on solid substrates;Colloids and Surfaces B: Biointerfaces;2018-07

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