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Showing 1 to 8 of 8 for “"PQC"”.

  1. Hrd1 Partners In Endoplasmic Reticulum-Associated Degradation

    <p>Protein Quality Control (PQC) comprises cellular pathways that regulate the turnover of short-lived, misfolded proteins. A main component of PQC is Endoplasmic Reticulum (ER)-Associated Degradation (ERAD), which controls the degradation of proteins synthesized in the ER. Aberrations in ERAD have …

    wayne-thes Repository record for Hrd1 Partners In Endoplasmic Reticulum-Associated Degradation (opens in a new tab)

  2. FPGA Implementation and Optimization of Bit Flipping Key Generation Algorithm for Post Quantum Cryptography in Embedded Systems Applications

    … systems, calling for post-quantum cryptography (PQC) solutions like Bit Flipping Key Encapsulation (BIKE) algorithm, which utilizes Quasi-Cyclic Moderate Density Parity-Check (QC-MCPC) codes for a secure key exchange. Even though BIKE has cryptographic strengths like structural simplicity, and …

    houston Repository record for FPGA Implementation and Optimization of Bit Flipping Key Generation Algorithm for Post Quantum Cryptography in Embedded Systems Applications (opens in a new tab)

  3. THE INTERPLAY BETWEEN THE PROTEIN QUALITY CONTROL SYSTEM AND EXTRACELLULAR VESICLES IN THE DISPOSAL OF DISEASE-ASSOCIATED PROTEINS AND MIRNAS IN ALS AND FTD MODELS

    … degradation through the protein quality control (PQC) system (i.e. chaperone and co-chaperone proteins, the ubiquitin proteasome system (UPS) and the autophagy). However, TDP-43 has been also found into extracellular vesicles (EVs), both large (LEVs) and small (SEVs), suggesting that EVs could …

    milano Repository record for THE INTERPLAY BETWEEN THE PROTEIN QUALITY CONTROL SYSTEM AND EXTRACELLULAR VESICLES IN THE DISPOSAL OF DISEASE-ASSOCIATED PROTEINS AND MIRNAS IN ALS AND FTD MODELS (opens in a new tab)

  4. Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease

    Protein quality control (pQC) in all cells is mediated by macromolecular machines that make new proteins, ensure that newly translated polypeptides are properly folded, and degrade aberrant proteins. Mechanoenzymes belonging to the AAA+ (ATPases associated with diverse cellular activities) …

    mit Repository record for Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease (opens in a new tab)

  5. The Phase Behavior of Ubqln Proteins and Implications for Protein Quality Control

    … for maintaining protein quality control (PQC) in cells. Misfolded proteins and large aggregates are cleared by UPS and autophagy signaled by ubiquitin (Ub) or polyubiquitin (polyUb) chains. Shuttle proteins facilitate cargo transporting by interacting with both ubiquitin and degradation …

    syracuse-diss Repository record for The Phase Behavior of Ubqln Proteins and Implications for Protein Quality Control (opens in a new tab)

  6. Impacto y Estrategia de Migración a Criptografía Post-Cuántica en Infraestructuras PKI Empresariales

    … migración hacia la Criptografía Post-Cuántica (PQC) en las infraestructuras de Clave Pública (PKI) empresariales. Ante la inminente amenaza Y2Q y los ataques de tipo "Harvest Now, Decrypt Later", el proyecto evalúa la viabilidad técnica de integrar los nuevos estándares post-cuánticos del NIST …

    catalunya Repository record for Impacto y Estrategia de Migración a Criptografía Post-Cuántica en Infraestructuras PKI Empresariales (opens in a new tab)

  7. Entropy Estimation for Arbiter PUF and Applications to Authenticated Key Exchange

    Physically Unclonable Functions (PUF) are hardware-based security primitives whose unique challenge and response behavior serves as a "fingerprint" for device authentication, key generation, and anti-counterfeiting. Modeling and estimating the entropy of PUF responses to random challenges is the …

    calgary Repository record for Entropy Estimation for Arbiter PUF and Applications to Authenticated Key Exchange (opens in a new tab)