Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Vaxxon SRP Salmonella-50 Dose
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Crystals | Free Full-Text | Tryptophan, an Amino-Acid Endowed with Unique Properties and Its Many Roles in Membrane Proteins
Sandbox porins - Proteopedia, life in 3D
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Analytical Approaches for Studying Transporters, Channels and Porins | Chemical Reviews
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Design, assembly, and characterization of membrane-spanning DNA nanopores | Nature Protocols
Outer Membrane Proteins | SpringerLink
Building membrane nanopores | Nature Nanotechnology
Analytical Approaches for Studying Transporters, Channels and Porins | Chemical Reviews
MCQ FOR PLANT PATHOLOGY ASRB NET / PREVIOUS PAPER PLANT PATHOLOGY/ MCQ FOR ICAR NET PLANT PATHOLOGY - YouTube
Rosette Nanotube Porins as Ion Selective Transporters and Single-Molecule Sensors | Journal of the American Chemical Society
Structure and functional mechanism of porins
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Analytical Approaches for Studying Transporters, Channels and Porins | Chemical Reviews
Analytical Approaches for Studying Transporters, Channels and Porins | Chemical Reviews
Robins & Morton (@RobinsMorton) / X
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Membrane Proteins & its types | PPT
Sandbox porins - Proteopedia, life in 3D
Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis | Chemical Reviews
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution - ScienceDirect
