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Structured Review

NanoTemper Technologies stability analysis software v1.0.3
Stability Analysis Software V1.0.3, supplied by NanoTemper Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/stability+analysis/pr+stability+analysis+software/us11739160-910-0-4
Average 90 stars, based on 1 article reviews
stability analysis software v1.0.3 - by Bioz Stars, 2026-10
90/100 stars

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other:

Article Title: Phylogenetically distinct fungal expansins show different binding preferences towards cellulosic materials and enhance cellulase activity
Article Snippet: ThermControl (NanoTemper Technologies) and the data were analyzed using the PR.Stability Analysis tool (NanoTemper Technologies).

Article Title: 4-Hydroxy-1α,25-Dihydroxyvitamin D 3 : Synthesis and Structure–Function Study
Article Snippet: NanoTemper PR.Stability Analysis v1.0.2 was used to fit the data and to determine melting temperatures Tm.

Article Title: A structural and mechanistic model for BSEP dysfunction in PFIC2 cholestatic disease.
Article Snippet: The resulting melting curves were analyzed with PR.Stability Analysis software (NanoTemper Technologies) to extract a melting temperature (Tm).

Article Title: Polypeptide comprising a single-domain antibody variable region that binds delta-like ligand 3 (DLL3) and method of use thereof to make a radionuclide complex
Article Snippet: Separation was performed using the HT Antibody Analysis 200 assay setting on the LabChipGXII Touch instrument (Perkin Elmer).

Article Title: Polypeptide comprising a single-domain antibody variable region that binds delta-like ligand 3 (DLL3) and method of use thereof to make a radionuclide complex
Article Snippet: The data was analyzed using the LabChip GX Reviewer Software (Perkin Elmer).

Article Title: FGFR1/KLB targeting agonistic antigen-binding proteins and conjugates thereof with GLP-1R agonistic peptides
Article Snippet: ThermControl Software v2.3.1 (Nanotemper Technologies) and analyzed using PR.Stability Analysis Software v1.0.3 (Nanotemper Technologies).

Article Title: Design, synthesis and biological evaluation of a novel non-Gemini analog of UVB1 and crystal structure of its complex with the vitamin D receptor.
Article Snippet: We synthesized UG-650, a novel non-Gemini analog of UVB1 that combines structural features of UVB1 andMC 1288.. The evaluation of the bioactivities indicates that UG-650 dose-dependently inhibited MCF-7 cell proliferation.. In comparison to calcitriol, slightly lower concentrations of UG-650 were needed to achieve equivalent levels of proliferation inhibition.

Fluorescence:

Article Title: Structural insights into the binding of nanobodies to the staphylococcal enterotoxin B.
Article Snippet: Staphylococcal Enterotoxin Type B (SEB), produced by Staphylococcus aureus bacteria, is notorious for inducing severe food poisoning and toxic shock syndrome.. While nanobody-based treatments hold promises for combating SEB-induced diseases, the lack of structural information between SEB and nanobodies has hindered the development of nanobody-based therapeutics.. Here, we present crystal structures of SEB-Nb3, SEB-Nb6, SEB-Nb8, SEB-Nb11, and SEB-Nb20 at resolutions ranging from 1.59 Å to 2.33 Å. Crystallographic analysis revealed that Nb3, Nb8, Nb11, and Nb20 bind to SEB at the T-cell receptor (TCR) interface, while Nb6 binds at the major histocompatibility complex (MHC) interface, suggesting their potential to inhibit SEB function by disrupting interactions with TCR or MHC molecules.

Stability:

Article Title: Structural insights into the binding of nanobodies to the staphylococcal enterotoxin B.
Article Snippet: Staphylococcal Enterotoxin Type B (SEB), produced by Staphylococcus aureus bacteria, is notorious for inducing severe food poisoning and toxic shock syndrome.. While nanobody-based treatments hold promises for combating SEB-induced diseases, the lack of structural information between SEB and nanobodies has hindered the development of nanobody-based therapeutics.. Here, we present crystal structures of SEB-Nb3, SEB-Nb6, SEB-Nb8, SEB-Nb11, and SEB-Nb20 at resolutions ranging from 1.59 Å to 2.33 Å. Crystallographic analysis revealed that Nb3, Nb8, Nb11, and Nb20 bind to SEB at the T-cell receptor (TCR) interface, while Nb6 binds at the major histocompatibility complex (MHC) interface, suggesting their potential to inhibit SEB function by disrupting interactions with TCR or MHC molecules.

Analysis:

Article Title: Structural insights into the binding of nanobodies to the staphylococcal enterotoxin B.
Article Snippet: Staphylococcal Enterotoxin Type B (SEB), produced by Staphylococcus aureus bacteria, is notorious for inducing severe food poisoning and toxic shock syndrome.. While nanobody-based treatments hold promises for combating SEB-induced diseases, the lack of structural information between SEB and nanobodies has hindered the development of nanobody-based therapeutics.. Here, we present crystal structures of SEB-Nb3, SEB-Nb6, SEB-Nb8, SEB-Nb11, and SEB-Nb20 at resolutions ranging from 1.59 Å to 2.33 Å. Crystallographic analysis revealed that Nb3, Nb8, Nb11, and Nb20 bind to SEB at the T-cell receptor (TCR) interface, while Nb6 binds at the major histocompatibility complex (MHC) interface, suggesting their potential to inhibit SEB function by disrupting interactions with TCR or MHC molecules.

Software:

Article Title: Structural insights into the binding of nanobodies to the staphylococcal enterotoxin B.
Article Snippet: Staphylococcal Enterotoxin Type B (SEB), produced by Staphylococcus aureus bacteria, is notorious for inducing severe food poisoning and toxic shock syndrome.. While nanobody-based treatments hold promises for combating SEB-induced diseases, the lack of structural information between SEB and nanobodies has hindered the development of nanobody-based therapeutics.. Here, we present crystal structures of SEB-Nb3, SEB-Nb6, SEB-Nb8, SEB-Nb11, and SEB-Nb20 at resolutions ranging from 1.59 Å to 2.33 Å. Crystallographic analysis revealed that Nb3, Nb8, Nb11, and Nb20 bind to SEB at the T-cell receptor (TCR) interface, while Nb6 binds at the major histocompatibility complex (MHC) interface, suggesting their potential to inhibit SEB function by disrupting interactions with TCR or MHC molecules.



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