Matches in SemOpenAlex for { <https://semopenalex.org/work/W4308437112> ?p ?o ?g. }
Showing items 1 to 84 of
84
with 100 items per page.
- W4308437112 abstract "Abstract Tyrosinase is the key enzyme (TYR) regulating melanin biosynthesis pathway and different TYR mutants had been shown to be retained within the Endoplasmic Reticulum (ER) in varying degrees, instead of being localized in the melanosome. Interestingly, a direct correlation could be ascertained between the enzyme activities of the mutants and their respective degrees of ER retentions (Moumita Chaki et al., 2011; Mondal, Sengupta, & Ray, 2016); but the molecular bases of such variations in retentions has largely been unknown. In the current study, for the very first time, we tried to check if structural constraints like – (i) position of an amino acid within TYR, whether buried or surface exposed (which is reflected by Accessible Surface Area value), (ii) change in nature of amino acid, (iii) changes in overall electrostatic potential (iv) changes in hydrogen bonding (v) steric hindrance (vi) change in overall stability due to non-synonymous amino acid substitutions have contributing effects upon differential retentions of the mutants within ER. To achieve our aim, we did homology models of 45 TYR variants that have previously been functionally characterized by Mondal, Sengupta, & Ray, 2016, with respect to their degrees of ER retentions, as well as their individual levels of enzyme activities. To our surprise, we did not get any correlations whatsoever between differential functional characteristics of mutant TYRs with differential structural attributes. This indicates towards the role of some hitherto unexplored mechanism of processing of mutant protein variants that contribute toward their differential functional outcomes." @default.
- W4308437112 created "2022-11-11" @default.
- W4308437112 creator A5017266613 @default.
- W4308437112 creator A5047030358 @default.
- W4308437112 creator A5074547216 @default.
- W4308437112 creator A5076811429 @default.
- W4308437112 date "2022-11-07" @default.
- W4308437112 modified "2023-09-27" @default.
- W4308437112 title "Common structural attributes of Tyrosinase variants are unlikely to determine differential retentions within Endoplasmic Reticulum: A modelling study with 45 variants" @default.
- W4308437112 cites W1031578623 @default.
- W4308437112 cites W1482971402 @default.
- W4308437112 cites W1747519124 @default.
- W4308437112 cites W1981021420 @default.
- W4308437112 cites W2015642465 @default.
- W4308437112 cites W2023407244 @default.
- W4308437112 cites W2027009970 @default.
- W4308437112 cites W2052483082 @default.
- W4308437112 cites W2053021234 @default.
- W4308437112 cites W2063602861 @default.
- W4308437112 cites W2064274217 @default.
- W4308437112 cites W2077174989 @default.
- W4308437112 cites W2127664904 @default.
- W4308437112 cites W2132540199 @default.
- W4308437112 cites W2132629607 @default.
- W4308437112 cites W2148135961 @default.
- W4308437112 cites W2150726150 @default.
- W4308437112 cites W2154714625 @default.
- W4308437112 cites W2518354333 @default.
- W4308437112 cites W2799847583 @default.
- W4308437112 cites W2952900264 @default.
- W4308437112 cites W3205993759 @default.
- W4308437112 cites W3207893114 @default.
- W4308437112 cites W4211196614 @default.
- W4308437112 cites W4226428451 @default.
- W4308437112 doi "https://doi.org/10.21203/rs.3.rs-2228674/v1" @default.
- W4308437112 hasPublicationYear "2022" @default.
- W4308437112 type Work @default.
- W4308437112 citedByCount "0" @default.
- W4308437112 crossrefType "posted-content" @default.
- W4308437112 hasAuthorship W4308437112A5017266613 @default.
- W4308437112 hasAuthorship W4308437112A5047030358 @default.
- W4308437112 hasAuthorship W4308437112A5074547216 @default.
- W4308437112 hasAuthorship W4308437112A5076811429 @default.
- W4308437112 hasBestOaLocation W43084371121 @default.
- W4308437112 hasConcept C104317684 @default.
- W4308437112 hasConcept C12554922 @default.
- W4308437112 hasConcept C143065580 @default.
- W4308437112 hasConcept C158617107 @default.
- W4308437112 hasConcept C181199279 @default.
- W4308437112 hasConcept C185592680 @default.
- W4308437112 hasConcept C201194858 @default.
- W4308437112 hasConcept C515207424 @default.
- W4308437112 hasConcept C55493867 @default.
- W4308437112 hasConcept C71240020 @default.
- W4308437112 hasConcept C86803240 @default.
- W4308437112 hasConcept C87554066 @default.
- W4308437112 hasConceptScore W4308437112C104317684 @default.
- W4308437112 hasConceptScore W4308437112C12554922 @default.
- W4308437112 hasConceptScore W4308437112C143065580 @default.
- W4308437112 hasConceptScore W4308437112C158617107 @default.
- W4308437112 hasConceptScore W4308437112C181199279 @default.
- W4308437112 hasConceptScore W4308437112C185592680 @default.
- W4308437112 hasConceptScore W4308437112C201194858 @default.
- W4308437112 hasConceptScore W4308437112C515207424 @default.
- W4308437112 hasConceptScore W4308437112C55493867 @default.
- W4308437112 hasConceptScore W4308437112C71240020 @default.
- W4308437112 hasConceptScore W4308437112C86803240 @default.
- W4308437112 hasConceptScore W4308437112C87554066 @default.
- W4308437112 hasLocation W43084371121 @default.
- W4308437112 hasOpenAccess W4308437112 @default.
- W4308437112 hasPrimaryLocation W43084371121 @default.
- W4308437112 hasRelatedWork W1999810095 @default.
- W4308437112 hasRelatedWork W2004312381 @default.
- W4308437112 hasRelatedWork W2013706919 @default.
- W4308437112 hasRelatedWork W2043316009 @default.
- W4308437112 hasRelatedWork W2086527094 @default.
- W4308437112 hasRelatedWork W2095128547 @default.
- W4308437112 hasRelatedWork W2341645127 @default.
- W4308437112 hasRelatedWork W2900504840 @default.
- W4308437112 hasRelatedWork W3131068657 @default.
- W4308437112 hasRelatedWork W214510971 @default.
- W4308437112 isParatext "false" @default.
- W4308437112 isRetracted "false" @default.
- W4308437112 workType "article" @default.