Results 1 to 10 of about 30,083 (177)

Induced Fit in Protein Multimerization: The HFBI Case. [PDF]

open access: yesPLoS Computational Biology, 2016
Hydrophobins, produced by filamentous fungi, are small amphipathic proteins whose biological functions rely on their unique surface-activity properties.
Laura Riccardi, Paolo Mereghetti
doaj   +5 more sources

Looking for Novel Capsid Protein Multimerization Inhibitors of Feline Immunodeficiency Virus [PDF]

open access: goldPharmaceuticals, 2018
Feline immunodeficiency virus (FIV) is a member of the retroviridae family of viruses. It causes acquired immunodeficiency syndrome (AIDS) in worldwide domestic and non-domestic cats and is a cause of an important veterinary issue.
Natalia Sierra   +5 more
doaj   +4 more sources

Designed protein multimerization and polymerization for functionalization of proteins. [PDF]

open access: yesBiotechnol Lett, 2022
Multimeric and polymeric proteins are large biomacromolecules consisting of multiple protein molecules as their monomeric units, connected through covalent or non-covalent bonds. Genetic modification and post-translational modifications (PTMs) of proteins offer alternative strategies for designing and creating multimeric and polymeric proteins ...
Permana D, Putra HE, Djaenudin D.
europepmc   +4 more sources

Stochastic protein multimerization, activity, and fitness. [PDF]

open access: yesPhys Rev E, 2018
Many proteins assemble into homomultimeric structures, with a number of subunits that can vary substantially among phylogenetic lineages. As protein-protein interactions require productive encounters among subunits, such variation might partially be explained by variation in cellular protein abundance. Protein abundance in turn depends on the intrinsic
Hagner K, Setayeshgar S, Lynch M.
europepmc   +4 more sources

Self-Multimerization of mRNA LNP-Derived Antigen Improves Antibody Responses [PDF]

open access: yesVaccines
Background: mRNA LNP technology is now being widely applied as a highly effective vaccine platform. Antigen multimerization is a well-established approach to enhance the antibody titers and protective efficacy of several protein subunit vaccines. However,
Cody A. Despins   +5 more
doaj   +3 more sources

ASPPs multimerize protein phosphatase 1. [PDF]

open access: greenPLOS Genetics
AbstractProtein Phosphatase 1 (PP1) activity is thought to be spatiotemporally defined by hundreds of different regulatory subunits, but their mechanisms of action are largely unknown. The Ankyrin repeat, SH3-domain, and Proline-rich region containing Proteins (ASPPs) bind and localize PP1 to cell-cell junctions.
Derek T. Wei (22446734)   +7 more
  +6 more sources

Functional multimerization of mucolipin channel proteins [PDF]

open access: bronzeJournal of Cellular Physiology, 2009
AbstractMCOLN1 encodes mucolipin‐1 (TRPML1), a member of the transient receptor potential TRPML subfamily of channel proteins. Mutations in MCOLN1 cause mucolipidosis‐type IV (MLIV), a lysosomal storage disorder characterized by severe neurologic, ophthalmologic, and gastrointestinal abnormalities.
Cyntia Curcio‐Morelli   +6 more
openalex   +4 more sources

The signal peptide of staphylococcal protein A alters the multimeric states of PepV [PDF]

open access: yesMicrobiology Spectrum
Signal peptides (SPs) have traditionally been recognized as molecular address tags that direct protein translocation between subcellular compartments. However, emerging evidence suggests that they serve additional functions beyond their canonical role in
Muhammad S. Azam, Dominique Missiakas
doaj   +2 more sources

The effect of exon 7 deletion during the evolution of TRIMCyp fusion proteins on viral restriction, cytoplasmic body formation and multimerization. [PDF]

open access: goldPLoS ONE, 2015
TRIMCyp is a fusion protein consisting of the TRIM5 gene product and retrotransposed Cyclophilin A (CypA). Two primate TRIMCyp fusion proteins with varying anti-HIV-1 activities independently evolved in owl monkeys and Old World monkeys. In addition, Old
Feng Liang Liu   +5 more
doaj   +3 more sources

Increase in cysteine-mediated multimerization under attractive protein–protein interactions

open access: hybridPreparative Biochemistry & Biotechnology, 2022
The CASPON enzyme became an interesting enzyme for fusion protein processing because it generates an authentic N-terminus. However, the high cysteine content of the CASPON enzyme may induce aggregation via disulfide-bond formation, which can reduce enzymatic activity and be considered a critical quality attribute.
Leo A. Jakob   +3 more
openalex   +3 more sources

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