Full Name
Kolatkar, Prasanna Ratnakar
(not current staff)
Variants
Kolatkar, P.
Kolatkar, P.R.
PRASANNA R KOLATKAR
 
Main Affiliation
 
 
Email
dbsprk@nus.edu.sg
 

Publications

Results 1-20 of 34 (Search time: 0.006 seconds).

Issue DateTitleAuthor(s)
130-Oct-2012A Divalent Ion Is Crucial in the Structure and Dominant-Negative Function of ID Proteins, a Class of Helix-Loop-Helix Transcription RegulatorsWong, M.V.; Jiang, S.; Palasingam, P.; Kolatkar, P.R. 
22006Analysis of 14 LRRK2 mutations in Parkinson's plus syndromes and late-onset Parkinson's diseaseTan E.-K. ; Skipper L.; Chua E.; Wong M.-C. ; Pavanni R. ; Bonnard C.; Kolatkar P. ; Liu J.-J.
32005Analysis of LRRK2 functional domains in nondominant Parkinson diseaseSkipper L.; Shen H.; Chua E.; Bonnard C.; Kolatkar P. ; Tan L.C.S. ; Jamora R.D.; Puvan K. ; Puong K.Y.; Zhao Y.; Pavanni R. ; Wong M.C. ; Yuen Y. ; Farrer M.; Liu J.J. ; Tan E.K. 
42002Androgen receptor mutations causing human androgen insensitivity syndromes show a key role of residue M807 in helix 8-helix 10 interactions and in receptor ligand-binding domain stabilityOng, Y.C.; Yong, E.L. ; Kolatkar, P.R. 
51999BioJAKE: a tool for the creation, visualization and manipulation of metabolic pathways.Salamonsen, W.; Mok, K.Y.; Kolatkar, P. ; Subbiah, S.
6Nov-2012Cloning, purification and preliminary X-ray data analysis of the human ID2 homodimerWong, M.V.; Palasingam, P.; Kolatkar, P.R. 
72003Compression of functional space in HLA-A sequence diversityZhao, B.; Sakharkar, M.K. ; Kangueane, P.; Png, A.E.H.; Ren, E.C. ; Kolatkar, P.R. ; Mathura, V.S.
8Jun-2011Conversion of Sox17 into a pluripotency reprogramming factor by reengineering its association with Oct4 on DNAJauch, R.; Aksoy, I.; Hutchins, A.P.; Ng, C.K.L.; Tian, X.F.; Chen, J.; Palasingam, P.; Robson, P.; Stanton, L.W.; Kolatkar, P.R. 
9Apr-2012Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206Liang, Y.; Choo, S.H.; Rossbach, M.; Baburajendran, N.; Palasingam, P.; Kolatkar, P.R. 
102009Crystal optimization and preliminary diffraction data analysis of the Smad1 MH1 domain bound to a palindromic SBE DNA elementBaburajendran, N.; Palasingam, P.; Ng, C.K.L.; Jauch, R.; Kolatkar, P.R. 
11Dec-1999Crystallization and preliminary crystallographic study of stonustoxin, a protein lethal factor isolated from the stonefish (Synanceja horrida) venomYew, W.S.; Kolatkar, P.R. ; Kuhn, P.; Khoo, H.E.
122003Crystallization and preliminary X-ray crystallographic studies on the fungal immunomodulatory protein Fve from the golden needle mushroom (Flammulina velutipes)Seow, S.V. ; Kuo, I.-C. ; Chua, K.Y. ; Paaventhan, P. ; Kolatkar, P.R. 
13Jun-2012Deciphering the Sox-Oct partner code by quantitative cooperativity measurementsNg, C.K.L.; Li, N.X.; Chee, S.; Prabhakar, S.; Kolatkar, P.R. ; Jauch, R.
141998Development of software tools at BioInformatics Centre (BIC) at the National University of Singapore (NUS).Kolatkar, P.R. ; Sakharkar, M.K. ; Tse, C.R.; Kiong, B.K. ; Wong, L.; Tan, T.W. ; Subbiah, S.
15Aug-2007Identification and characterization of a novel mutation in the carbonic anhydrase IV gene that causes retinitis pigmentosaAlvarez, B.V.; Vithana, E.N. ; Yang, Z.; Koh, A.H.; Yeung, K.; Yong, V.; Shandro, H.J.; Chen, Y.; Kolatkar, P. ; Palasingam, P.; Zhang, K.; Aung, T. ; Casey, J.R.
1617-Jun-2011Identification of a polyoxometalate inhibitor of the DNA binding activity of sox2Narasimhan, K.; Pillay, S.; Bin Ahmad, N.R.; Bikadi, Z.; Hazai, E.; Yan, L.; Kolatkar, P.R. ; Pervushin, K.; Jauch, R.
172000IE-Kb: Intron exon knowledge baseSakharkar, M.K. ; Kangueane, P.; Woon, T.W. ; Tan, T.W. ; Kolatkar, P.R. ; Long, M.; De Souza, S.J.
181998Integration of bioinformatics tools at the National University of Singapore (NUS)Kolatkar, P.R. ; Sakharkar, M.K. ; Roderic, T.C.; Kiong, B.K. ; Wong, L.; Tan, T.W. ; Subbiah, S.
191998Integration of bioInformatics tools at the National University of Singapore (NUS).Kolatkar, P.R. ; Sakharkar, M.K. ; Roderic, T.C.; Kiong, B.K. ; Wong, L.; Tan, T.W. ; Subbiah, S.
2030-Oct-1998Interconversion of the kinetic identities of the tandem catalytic domains of receptor-like protein-tyrosine phosphatase PTPα by two point mutations is synergistic and substrate-dependentLim, K.L.; Kolatkar, P.R. ; Ng, K.P.; Ng, C.H.; Pallen, C.J.