These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

436 related articles for article (PubMed ID: 32103094)

  • 1. Taurine Induces an Ordered but Functionally Inactive Conformation in Intrinsically Disordered Casein Proteins.
    Bhat MY; Singh LR; Dar TA
    Sci Rep; 2020 Feb; 10(1):3503. PubMed ID: 32103094
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Trimethylamine N-oxide alters structure-function integrity of β-casein: Structural disorder co-regulates the aggregation propensity and chaperone activity.
    Bhat MY; Malik MA; Singh LR; Dar TA
    Int J Biol Macromol; 2021 Jul; 182():921-930. PubMed ID: 33872615
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Disorder under stress: Role of polyol osmolytes in modulating fibrillation and aggregation of intrinsically disordered proteins.
    Verma G; Singh P; Bhat R
    Biophys Chem; 2020 Sep; 264():106422. PubMed ID: 32707418
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Conformational properties of intrinsically disordered proteins bound to the surface of silica nanoparticles.
    Vitali M; Rigamonti V; Natalello A; Colzani B; Avvakumova S; Brocca S; Santambrogio C; Narkiewicz J; Legname G; Colombo M; Prosperi D; Grandori R
    Biochim Biophys Acta Gen Subj; 2018 Jul; 1862(7):1556-1564. PubMed ID: 29621630
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Conformational transition of κ-casein in micellar environment: Insight from the tryptophan fluorescence.
    Mishra S; Meher G; Chakraborty H
    Spectrochim Acta A Mol Biomol Spectrosc; 2017 Nov; 186():99-104. PubMed ID: 28622544
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Trimethylamine N-oxide abolishes the chaperone activity of α-casein: an intrinsically disordered protein.
    Bhat MY; Singh LR; Dar TA
    Sci Rep; 2017 Jul; 7(1):6572. PubMed ID: 28747709
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.
    Fonin AV; Darling AL; Kuznetsova IM; Turoverov KK; Uversky VN
    Cell Mol Life Sci; 2018 Nov; 75(21):3907-3929. PubMed ID: 30066087
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.
    Yang J; Gao M; Xiong J; Su Z; Huang Y
    Protein Sci; 2019 Nov; 28(11):1952-1965. PubMed ID: 31441158
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell.
    Deiana A; Forcelloni S; Porrello A; Giansanti A
    PLoS One; 2019; 14(8):e0217889. PubMed ID: 31425549
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Functional and dysfunctional folding, association and aggregation of caseins.
    Carver JA; Holt C
    Adv Protein Chem Struct Biol; 2019; 118():163-216. PubMed ID: 31928725
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Folding propensity of intrinsically disordered proteins by osmotic stress.
    Mansouri AL; Grese LN; Rowe EL; Pino JC; Chennubhotla SC; Ramanathan A; O'Neill HM; Berthelier V; Stanley CB
    Mol Biosyst; 2016 Nov; 12(12):3695-3701. PubMed ID: 27752679
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Dynamics and rigidity in an intrinsically disordered protein, β-casein.
    Perticaroli S; Nickels JD; Ehlers G; Mamontov E; Sokolov AP
    J Phys Chem B; 2014 Jul; 118(26):7317-26. PubMed ID: 24918971
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Conservation and coevolution determine evolvability of different classes of disordered residues in human intrinsically disordered proteins.
    Basu S; Bahadur RP
    Proteins; 2022 Mar; 90(3):632-644. PubMed ID: 34626492
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Templated folding of intrinsically disordered proteins.
    Toto A; Malagrinò F; Visconti L; Troilo F; Pagano L; Brunori M; Jemth P; Gianni S
    J Biol Chem; 2020 May; 295(19):6586-6593. PubMed ID: 32253236
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Do sequence neighbours of intrinsically disordered regions promote structural flexibility in intrinsically disordered proteins?
    Basu S; Bahadur RP
    J Struct Biol; 2020 Feb; 209(2):107428. PubMed ID: 31756456
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Effect of polyols on the structure and aggregation of recombinant human γ-Synuclein, an intrinsically disordered protein.
    Roy S; Bhat R
    Biochim Biophys Acta Proteins Proteom; 2018 Oct; 1866(10):1029-1042. PubMed ID: 30003969
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Proteins without unique 3D structures: biotechnological applications of intrinsically unstable/disordered proteins.
    Uversky VN
    Biotechnol J; 2015 Mar; 10(3):356-66. PubMed ID: 25287424
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Recent advances in atomic molecular dynamics simulation of intrinsically disordered proteins.
    Wang W
    Phys Chem Chem Phys; 2021 Jan; 23(2):777-784. PubMed ID: 33355572
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Reshaping the protein folding pathway by osmolyte via its effects on the folding intermediates.
    Sharma GS; Dar TA; Singh LR
    Curr Protein Pept Sci; 2015; 16(6):513-20. PubMed ID: 26100280
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.
    Arai M; Sugase K; Dyson HJ; Wright PE
    Proc Natl Acad Sci U S A; 2015 Aug; 112(31):9614-9. PubMed ID: 26195786
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 22.