Search Results - "Atreya, H. S."

NMR Derived Solution Structure of an EF-Hand Calcium-Binding Protein from Entamoeba Histolytica by Atreya, H. S, Sahu, S. C, Bhattacharya, A, Govil, Girjesh

“…We present the three-dimensional (3D) solution structure of a calcium-binding protein from Entamoeba histolytica (EhCaBP), an etiologic agent of amoebiasis…”
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A tracked approach for automated NMR assignments in proteins (TATAPRO) by Atreya, H S, Sahu, S C, Chary, K V, Govil, G

“…A novel automated approach for the sequence specific NMR assignments of 1HN, 13Calpha, 13Cbeta, 13C'/1Halpha and 15N spins in proteins, using triple resonance…”
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A pyrrole-based natural small molecule mitigates HSP90 expression in MDA-MB-231 cells and inhibits tumor angiogenesis in mice by inactivating HSF-1 by Rashmi, K. C., Atreya, H. S., Raj, M. Harsha, Salimath, Bharathi P., Aparna, H. S.

“…Heat shock proteins (HSPs), molecular chaperones, are crucial for the cancer cells to facilitate proper functioning of various oncoproteins involved in cell…”
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Automated NMR assignments of proteins for high throughput structure determination: TATAPRO II by Atreya, H. S., Chary, K. V. R., Govil, Girjesh

“…TATAPRO (Tracked Automated Assignments in Proteins), a novel algorithm for automated NMR assignments in proteins is presented to aid in high throughput protein…”
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New chemical shift signatures of bound calcium in EF-hand proteins by Atreya, H. S., Chary, K. V. R.

“…We present two new chemical shift signatures for monitoring the state of bound calcium (Ca2+) in NMR studies of EF-hand proteins. They have been observed in…”
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Structure determination of proteins in solution by nuclear magnetic resonance spectroscopy by Chary, K V R, Atreya, H S

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Amino acid selective 'unlabelling' for residue-specific NMR assignments in proteins by Atreya, H. S., Chary, K. V. R.

“…A novel methodology for sequence-specific resonance assignments in proteins, using amino acid selective 'unlabelling' is presented. The strategy is based on…”
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Rapid NMR data collection by Atreya, Hanudatta S, Szyperski, Thomas

“…Rapid data collection is an area of intense research in biomolecular NMR spectroscopy, in particular for high-throughput structure determination in structural…”
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G-Matrix Fourier Transform NMR Spectroscopy for Complete Protein Resonance Assignment by Atreya, Hanudatta S., Szyperski, Thomas, Hauptman, Herbert

“…A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. Each of the GFT NMR experiments presented…”
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Helical Aromatic Oligoamides:  Reliable, Readily Predictable Folding from the Combination of Rigidified Structural Motifs by Yuan, Lihua, Zeng, Huaqiang, Yamato, Kazuhiro, Sanford, Adam R, Feng, Wen, Atreya, Hanudatta S, Sukumaran, Dinesh K, Szyperski, Thomas, Gong, Bing

“…Factors responsible for the folding of aromatic oligoamides with backbones rigidified by local three-center H-bonds were investigated. The stability of the…”
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NMR Data Collection and Analysis Protocol for High-Throughput Protein Structure Determination by Liu, Gaohua, Shen, Yang, Atreya, Hanudatta S., Parish, David, Shao, Ying, Sukumaran, Dinesh K., Xiao, Rong, Yee, Adelinda, Lemak, Alexander, Bhattacharya, Aneerban, Acton, Thomas A., Arrowsmith, Cheryl H., Montelione, Gaetano T., Szyperski, Thomas, Hendrickson, Wayne A.

“…A standardized protocol enabling rapid NMR data collection for high-quality protein structure determination is presented that allows one to capitalize on high…”
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G-Matrix Fourier Transform NOESY-Based Protocol for High-Quality Protein Structure Determination by Shen, Yang, Atreya, Hanudatta S, Liu, Gaohua, Szyperski, Thomas

“…A protocol for high-quality structure determination based on G-matrix Fourier transform (GFT) NMR is presented. Five through-bond chemical shift correlation…”
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Measurement of 1J(Ni,Calpha(i)), 1J(Ni,C'i-1), 2J(Ni,Calpha(i-1)), 2J(H(N)i,C'i-1) and 2J(H(N)i,Calpha(i)) values in 13C/15N-labeled proteins by Mukherjee, Sulakshana, Mustafi, Sourajit M, Atreya, H S, Chary, K V R

“…Use of partial or selective (13)C/(15)N labeling of specific amino acid residues in a given protein to measure the values of (1)J((15)N(i),(13)C(alpha) (i)),…”
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Measurement of 1 J (N i ,C α i ), 1 J (N i ,C′ i −1 ), 2 J (N i ,C α i −1 ), 2 J (H N i ,C′ i −1 ) and 2 J (H N i ,C α i ) values in 13 C/ 15 N‐labeled proteins by Mukherjee, Sulakshana, Mustafi, Sourajit M., Atreya, H. S., Chary, K. V. R.

“…Abstract Use of partial or selective 13 C/ 15 N labeling of specific amino acid residues in a given protein to measure the values of 1 J ( 15 N i , 13 C α i ),…”
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Measurement of 1J(Ni,Cαi), 1J(Ni,C′i−1), 2J(Ni,Cαi−1), 2J(HNi,C′i−1) and 2J(HNi,Cαi) values in 13C/15N-labeled proteins by Mukherjee, Sulakshana, Mustafi, Sourajit M., Atreya, H. S., Chary, K. V. R.

“…Use of partial or selective 13C/15N labeling of specific amino acid residues in a given protein to measure the values of 1J(15Ni,13Cαi), 2J(1HN,13Cαi),…”
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Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues by Atreya, H S, Chary, K V

“…A novel methodology for stereospecific NMR assignments of methyl (CH3) groups of Val and Leu residues in fractionally 13C-labeled proteins is presented. The…”
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Sequence-specific 1H, 13C and 15N assignments of a calcium binding protein from Entamoeba histolytica by Sahu, S C, Atreya, H S, Chauhan, S, Bhattacharya, A, Chary, K V, Govil, G

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NMR structure of the 18 kDa protein CC1736 from Caulobacter crescentus identifies a member of the "START" domain superfamily and suggests residues mediating substrate specificity by Shen, Yang, Goldsmith-Fischman, Sharon, Atreya, Hanudatta S., Acton, Thomas, Ma, LiChung, Xiao, Rong, Honig, Barry, Montelione, Gaetano T., Szyperski, Thomas

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Technology Review - Structure Determination of Proteins in Solution by Nuclear Magnetic Resonance Spectroscopy by Chary KVR, Atreya HS

“…Each cell in the human body consists of a myriad of biological macromolecules and organelles, which are required for various cellular functions and metabolism…”
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GFT NMR based resonance assignment for the 21 kDa human protein UFC1 by Liu, Gaohua, Aramini, James, Atreya, Hanudatta S, Eletsky, Alexander, Xiao, Rong, Acton, Thomas, Ma, Lichung, Montelione, Gaetano T, Szyperski, Thomas

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