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This study presents an engineered human interferon‐lambda (hIFN‐λ) as an intranasal prophylactic against respiratory viruses. By combining AI‐guided backbone redesign and glycoengineering, the authors developed a thermostable, protease‐resistant, and scalable variant with improved mucosal penetration.
Jeongwon Yun +12 more
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Platelet Microtubule Subunit Proteins
Thrombosis and Haemostasis, 1979SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS ...
A G, Castle, N, Crawford
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Foldable subunits of helix protein
Computational Biology and Chemistry, 2009Detection of foldable subunits in proteins is an important approach to understand their evolutions and find building motifs for de novo protein design. Using united-residue model, we simulated the folding of a six-helix protein with a length of 120 amino acids (C-terminal domain of Ku86).
Yi, He +3 more
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The Rubisco subunit binding protein
Photosynthesis Research, 1988Chloroplasts contain an abundant soluble protein that binds non-covalently newly synthesized large and small subunits of the enzyme ribulose bisphosphate carboxylase-oxygenase. This binding protein has been purified from Pisum sativum and Hordeum vulgare in the form of a dodecamer consisting of equal amounts of two types of subunit.
R J, Ellis, S M, Van Der Vies
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Protein Circlets as Sex Pilus Subunits
Current Protein & Peptide Science, 2004The largest circular protein structures discovered define a class of transfer proteins acting in bacterial conjugation and type IV secretion. Proteins ranging from 73 to 78 residues with head-to-tail peptide bonds constitute the major subunit of conjugative pili of some type IV secretion systems.
Kalkum, M., Eisenbrandt, R., Lanka, E.
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Biochemical and Biophysical Research Communications, 1970
Abstract A method is described for studying spatially isolated subunits by attaching them covalently to a rigid matrix and thus preventing them from re-association. Application of this method to rabbit muscle aldolase indicates that the subunits are capable of enzyme activity.
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Abstract A method is described for studying spatially isolated subunits by attaching them covalently to a rigid matrix and thus preventing them from re-association. Application of this method to rabbit muscle aldolase indicates that the subunits are capable of enzyme activity.
openaire +2 more sources

