389 related articles for article (PubMed ID: 28525590)
1. SDM: a server for predicting effects of mutations on protein stability.
Pandurangan AP; Ochoa-Montaño B; Ascher DB; Blundell TL
Nucleic Acids Res; 2017 Jul; 45(W1):W229-W235. PubMed ID: 28525590
[TBL] [Abstract][Full Text] [Related]
2. SDM--a server for predicting effects of mutations on protein stability and malfunction.
Worth CL; Preissner R; Blundell TL
Nucleic Acids Res; 2011 Jul; 39(Web Server issue):W215-22. PubMed ID: 21593128
[TBL] [Abstract][Full Text] [Related]
3. DUET: a server for predicting effects of mutations on protein stability using an integrated computational approach.
Pires DE; Ascher DB; Blundell TL
Nucleic Acids Res; 2014 Jul; 42(Web Server issue):W314-9. PubMed ID: 24829462
[TBL] [Abstract][Full Text] [Related]
4. mCSM-NA: predicting the effects of mutations on protein-nucleic acids interactions.
Pires DEV; Ascher DB
Nucleic Acids Res; 2017 Jul; 45(W1):W241-W246. PubMed ID: 28383703
[TBL] [Abstract][Full Text] [Related]
5. SAAFEC-SEQ: A Sequence-Based Method for Predicting the Effect of Single Point Mutations on Protein Thermodynamic Stability.
Li G; Panday SK; Alexov E
Int J Mol Sci; 2021 Jan; 22(2):. PubMed ID: 33435356
[TBL] [Abstract][Full Text] [Related]
6. Protein Repair and Analysis Server: A Web Server to Repair PDB Structures, Add Missing Heavy Atoms and Hydrogen Atoms, and Assign Secondary Structures by Amide Interactions.
Nnyigide OS; Nnyigide TO; Lee SG; Hyun K
J Chem Inf Model; 2022 Sep; 62(17):4232-4246. PubMed ID: 36000562
[TBL] [Abstract][Full Text] [Related]
7. NCI: A server to identify non-canonical interactions in protein structures.
Babu MM
Nucleic Acids Res; 2003 Jul; 31(13):3345-8. PubMed ID: 12824323
[TBL] [Abstract][Full Text] [Related]
8. DynaMut2: Assessing changes in stability and flexibility upon single and multiple point missense mutations.
Rodrigues CHM; Pires DEV; Ascher DB
Protein Sci; 2021 Jan; 30(1):60-69. PubMed ID: 32881105
[TBL] [Abstract][Full Text] [Related]
9. DDMut: predicting effects of mutations on protein stability using deep learning.
Zhou Y; Pan Q; Pires DEV; Rodrigues CHM; Ascher DB
Nucleic Acids Res; 2023 Jul; 51(W1):W122-W128. PubMed ID: 37283042
[TBL] [Abstract][Full Text] [Related]
10. MutationExplorer: a webserver for mutation of proteins and 3D visualization of energetic impacts.
Philipp M; Moth CW; Ristic N; Tiemann JKS; Seufert F; Panfilova A; Meiler J; Hildebrand PW; Stein A; Wiegreffe D; Staritzbichler R
Nucleic Acids Res; 2024 Jul; 52(W1):W132-W139. PubMed ID: 38647044
[TBL] [Abstract][Full Text] [Related]
11. Machine learning integration for predicting the effect of single amino acid substitutions on protein stability.
Ozen A; Gönen M; Alpaydan E; Haliloğlu T
BMC Struct Biol; 2009 Oct; 9():66. PubMed ID: 19840377
[TBL] [Abstract][Full Text] [Related]
12. Predicting folding free energy changes upon single point mutations.
Zhang Z; Wang L; Gao Y; Zhang J; Zhenirovskyy M; Alexov E
Bioinformatics; 2012 Mar; 28(5):664-71. PubMed ID: 22238268
[TBL] [Abstract][Full Text] [Related]
13. WS-SNPs&GO: a web server for predicting the deleterious effect of human protein variants using functional annotation.
Capriotti E; Calabrese R; Fariselli P; Martelli PL; Altman RB; Casadio R
BMC Genomics; 2013; 14 Suppl 3(Suppl 3):S6. PubMed ID: 23819482
[TBL] [Abstract][Full Text] [Related]
14. TKSA-MC: A web server for rational mutation through the optimization of protein charge interactions.
Contessoto VG; de Oliveira VM; Fernandes BR; Slade GG; Leite VBP
Proteins; 2018 Nov; 86(11):1184-1188. PubMed ID: 30218467
[TBL] [Abstract][Full Text] [Related]
15. ANOLEA: a www server to assess protein structures.
Melo F; Devos D; Depiereux E; Feytmans E
Proc Int Conf Intell Syst Mol Biol; 1997; 5():187-90. PubMed ID: 9322034
[TBL] [Abstract][Full Text] [Related]
16. ProFunc: a server for predicting protein function from 3D structure.
Laskowski RA; Watson JD; Thornton JM
Nucleic Acids Res; 2005 Jul; 33(Web Server issue):W89-93. PubMed ID: 15980588
[TBL] [Abstract][Full Text] [Related]
17. Computational tools help improve protein stability but with a solubility tradeoff.
Broom A; Jacobi Z; Trainor K; Meiering EM
J Biol Chem; 2017 Sep; 292(35):14349-14361. PubMed ID: 28710274
[TBL] [Abstract][Full Text] [Related]
18. ReadOut: structure-based calculation of direct and indirect readout energies and specificities for protein-DNA recognition.
Ahmad S; Kono H; Araúzo-Bravo MJ; Sarai A
Nucleic Acids Res; 2006 Jul; 34(Web Server issue):W124-7. PubMed ID: 16844974
[TBL] [Abstract][Full Text] [Related]
19. Protein stability: a single recorded mutation aids in predicting the effects of other mutations in the same amino acid site.
Wainreb G; Wolf L; Ashkenazy H; Dehouck Y; Ben-Tal N
Bioinformatics; 2011 Dec; 27(23):3286-92. PubMed ID: 21998155
[TBL] [Abstract][Full Text] [Related]
20. SAAMBE: Webserver to Predict the Charge of Binding Free Energy Caused by Amino Acids Mutations.
Petukh M; Dai L; Alexov E
Int J Mol Sci; 2016 Apr; 17(4):547. PubMed ID: 27077847
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
