A5056850102- Historical Studies and Socio-cultural Analysis
- French Urban and Social Studies
- European Political History Analysis
- Protein Structure and Dynamics
- Enzyme Structure and Function
- French Historical and Cultural Studies
- Historical Economic and Social Studies
- Monoclonal and Polyclonal Antibodies Research
- RNA and protein synthesis mechanisms
- Social Sciences and Governance
- Bacteriophages and microbial interactions
- Fungal and yeast genetics research
- Chemical Synthesis and Analysis
- Historical and Literary Studies
- Education, sociology, and vocational training
- Multiculturalism, Politics, Migration, Gender
- Microtubule and mitosis dynamics
- Historical and Literary Analyses
- Glycosylation and Glycoproteins Research
- Cultural Identity and Heritage
- Historical Economic and Legal Thought
- Aging, Elder Care, and Social Issues
- Biochemical and Structural Characterization
- Social Policies and Family
- 14-3-3 protein interactions
Institutions et Dynamiques Historiques de l'Économie et de la Société
2011-2024
Université Paris 8
2010-2024
Université Paris-Saclay
2006-2023
Institut de Biologie Intégrative de la Cellule
2013-2023
Centre National de la Recherche Scientifique
2013-2023
CEA Paris-Saclay
2017-2023
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2015-2023
Université Paris Nanterre
2017-2023
École des hautes études en sciences sociales
1998-2021
Université Paris-Sud
2010-2020
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Engineered bacteria promise to revolutionize diagnostics and therapeutics, yet many applications are precluded by the limited number of detectable signals. Here we present a general framework engineer synthetic receptors enabling bacterial cells respond novel ligands. These activated via ligand-induced dimerization single-domain antibody fused monomeric DNA-binding domains (split-DBDs). Using E. coli as model system, both transmembrane cytosolic using VHH for ligand detection demonstrate...
Proteins are the most specific yet versatile biological self-assembling agents with a rich chemistry. Nevertheless, design of new proteins recognition capacities is still in its infancy and has seldom been exploited for self-assembly functional inorganic nanoparticles. Here, we report on protein-directed assembly gold nanoparticles using purpose-designed artificial repeat having rigid but modular 3D architecture. αRep protein pairs selected their high mutual affinity from library 109...
We previously designed a new family of artificial proteins named αRep based on subgroup thermostable helicoidal HEAT-like repeats. have now assembled large optimized library. In this library, the side chains at each variable position are not fully randomized but instead encoded by distribution codons natural frequency repeats family. The library construction is polymerization micro-genes and therefore results in with number improved process using "filtration" procedure to retain only coding...
Phox homology (PX) domains have been recently identified in a number of different proteins and are involved various cellular functions such as vacuolar targeting membrane protein trafficking. It was shown that these modules about 130 amino acids specifically binding to phosphoinositides this interaction is crucial for their function. The yeast genome contains 17 PX domain proteins. One these, Grd19p, the localization late Golgi DPAP A Kex2p. Grd19p consists with 30 extra residues at...
A new over‐expression system has been set up for Escherichia coli thioredoxin, yielding 55 mg purified protein/10 g fresh cells. This used to produce thioredoxin modified by site‐directed mutagenesis. Taking advantage of the structural and enzymatic similarity between E. spinach m ‐type Asp61 changed into Asn in order investigate impact suppression a charged residue on interaction with target enzymes. The modification did not significantly alter structure protein. Neither rate reduction...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCharacterization of an intermediate in the folding pathway phosphoglycerate kinase: Chemical reactivity genetically introduced cysteinyl residues during processNathalie Ballery, Michel Desmadril, Philippe Minard, and Jeannine M. YonCite this: Biochemistry 1993, 32, 2, 708–714Publication Date (Print):January 19, 1993Publication History Published online1 May 2002Published inissue 19 January...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTUnfolding-refolding of the domains in yeast phosphoglycerate kinase: comparison with isolated engineered domainsDominique Missiakas, Jean Michel Betton, Philippe Minard, and Jeannine M. YonCite this: Biochemistry 1990, 29, 37, 8683–8689Publication Date (Print):September 18, 1990Publication History Published online1 May 2002Published inissue 18 September...
Neocarzinostatin (NCS) is a small "all beta" protein displaying the same overall fold as immunoglobulins. This possesses well-defined hydrophobic core and two loops structurally equivalent to CDR1 CDR3 of NCS most studied member enediynechromoprotein family, clinically used an antitumoral agent. has promise drug delivery vehicle if new binding specificities could be conferred on its scaffold. Previous studies have shown that specificity crevasse can extended compounds completely unrelated...
The two domains of yeast phosphoglycerate kinase were produced by recombinant techniques. N-domain was obtained the introduction a termination codon at position coding for Phe185, and C-domain deletion in gene sequence between Serl Leu186. Both efficiently expressed yeast, level being greater than that N-domain. found to have quasi-native structure; retained its ability bind nucleotides. Small local differences detected domain structure compared whole enzyme, probably due lack interdomain...
Abstract Background Ankyrins are cellular mediators of a number essential protein-protein interactions. Unlike intrabodies, ankyrins composed highly structured repeat modules characterized by disulfide bridge-independent folding. Artificial ankyrin molecules, designed to target viral components, might act as intracellular antiviral agents and contribute the immunity against pathogens such HIV-1. Results A phage-displayed library artificial was constructed, screened on polyprotein made fused...
A family of artificial proteins, named αRep, based on a natural helical repeat was previously designed. αRep members are efficiently expressed, folded and extremely stable proteins. large library constructed creating proteins with randomized interaction surface. In the present study, we show that is an efficient source tailor-made specific direct applications in biochemistry cell biology. From this library, selected by phage display binders nanomolar dissociation constants against GFP. The...
Although antibodies remain a primary recognition element in all forms of biosensing, functional limitations arising from their size, stability, and structure have motivated the development production many different artificial scaffold proteins for biological recognition. However, implementing such binders into high-performance biosensors remains challenging task. Here, we present design application Förster resonance energy transfer (FRET) nanoprobes comprising small (αRep bidomains) labeled...
Long insertions into a loop of folded host protein are expected to have destabilizing effects because the entropic cost associated with closure unless inserted sequence adopts structure amino- and carboxy-termini in close proximity. A entropy reduction screen based on this concept was used an attempt retrieve sequences from random libraries. library long SH2 domain, displayed surface M13 phage, that did not disrupt function were retrieved by panning using beads coated phosphotyrosine...
Experiments were designed to explore the tolerance of protein structure and folding very large insertions folded within a structural domain. Dihydrofolate reductase β-lactamase have been inserted in four different positions phosphoglycerate kinase. The resultant chimeric proteins are all overexpressed, host as well partners functional. Although not explicitly designed, functional coupling between two fused was observed some chimeras. These results show that structures structured is more...
αRep is a family of entirely artificial repeat proteins. Within the previously described library, some variants are homodimers displaying interdomain cavities. Taking advantage these properties, one called A3 was converted into single chain bidomain metalloenzymes. A nonmutated domain covalently linked with an A3′ bearing unique cysteine on chosen mutated position (F119C or Y26C). This mutation ensured covalent coupling 1:1 copper(II)/phenanthroline copper(II)/terpyridine complex as...
Hybrid nanostructures are constructed by the direct coupling of fluorescent quantum dots and plasmonic gold nanoparticles. Self-assembly is directed strong affinity between two artificial α-repeat proteins that introduced in capping layers nanoparticles at a controlled surface density. The have been engineered to exhibit high mutual affinity, corresponding dissociation constant nanomolar range, towards protein-functionalized Protein-mediated self-assembly evidenced plasmon resonance gel...
Abstract Scaffold-based protein libraries are designed to be both diverse and rich in functional/folded proteins. However, introducing an extended diversity while preserving stability of the initial scaffold remains a challenge. Here we developed original approach select ensemble folded proteins from library. The thermostable CheY Thermotoga maritima was chosen as scaffold. Four loops were diversified create new binding surface. subset library giving rise first selected using natural partner...
Neocarzinostatin is the most studied member of enediyne-chromoprotein family, and clinically used as an antitumoral agent. could be a promising drug delivery vehicle if new binding specificities conferred to its protein scaffold. We in vitro evolution methods demonstrate that this approach feasible. created large libraries containing between 1.7 × 108 1.4 109 independent clones, where up 13 side chains pointing toward crevice were randomly substituted. then phage display select variants bind...
Site-specific mutants of yeast phosphoglycerate kinase have been produced in order to investigate the roles 'basic-patch' residues, arginine 168 and histidine 170. The fully-conserved residue, 168, has replaced with a lysine (R168K) methionine (R168M) while non-conserved 170 an aspartate (H170D). Comparison 500-MHz 1H-NMR spectra mutant proteins that wild-type shows overall fold remains essentially unaltered from native enzyme. Results NOE experiments indicate there are only very minor...