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RSS feed26  publications found

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1. Molecular imaging of breast tumors using a near-infrared fluorescently labeled clusterin binding peptide NPArC # 20217044  
Search for Filfil, Rana; Search for Paul-Roc, Béatrice; Search for Cantin, Christiane; Search for Iqbal, Umar; Search for Tolkatchev, Dmitri; Search for Vinogradova, Anna; Search for Xu, Ping; Search for Ni, Feng; Search for O'Connor-McCourt, Maureen D.; Search for Lenferink, Anne E. G.
International Journal of Cancer, 131 (5), 2012-01-27, p. E681-E692
Resolve DOI: http://dx.doi.org/10.1002/ijc.27368
Find@CISTI Molecular imaging of breast tumors using a near-infrared fluorescently labeled clusterin binding peptide NPArC # 20217044 (Opens in a new window)Find@CISTI Molecular imaging of breast tumors using a near-infrared fluorescently labeled clusterin binding peptide NPArC # 20217044
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Share It Molecular imaging of breast tumors using a near-infrared fluorescently labeled clusterin binding peptide NPArC # 20217044
 
2. Roles for endothelin receptor B and BCL2A1 in spontaneous CNS metastasis of melanoma NPArC # 20603072  
Search for Cruz-Munoz, William; Search for Jaramillo, Maria L.; Search for Man, Shan; Search for Xu, Ping; Search for Banville, Myriam; Search for Collins, Catherine; Search for Nantel, Andre; Search for Morgan, Sherif S.; Search for Cranmer, Lee D.; Search for O'Connor-McCourt, Maureen D.; Search for Kerbel, Robert S.
Cancer Research, 2012-08-03, p. 1-29
Resolve DOI: http://dx.doi.org/10.1158/0008-5472.CAN-12-2194
Find@CISTI Roles for endothelin receptor B and BCL2A1 in spontaneous CNS metastasis of melanoma NPArC # 20603072 (Opens in a new window)Find@CISTI Roles for endothelin receptor B and BCL2A1 in spontaneous CNS metastasis of melanoma NPArC # 20603072
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Share It Roles for endothelin receptor B and BCL2A1 in spontaneous CNS metastasis of melanoma NPArC # 20603072
 
3. Binding of human angiogenin inhibits actin polymerization NPArC # 16499153  
Search for Pyatibratov, Mikhail G.; Search for Tolkatchev, Dmitri; Search for Plamondon, Josee; Search for Xu, Ping; Search for Ni, Feng; Search for Kostyukova, Alla S.
Archives of biochemistry and biophysics, 495 (1), 2010-01-04, p. 74-81
Resolve DOI: http://dx.doi.org/10.1016/j.abb.2009.12.024
Find@CISTI Binding of human angiogenin inhibits actin polymerization NPArC # 16499153 (Opens in a new window)Find@CISTI Binding of human angiogenin inhibits actin polymerization NPArC # 16499153
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View full text Binding of human angiogenin inhibits actin polymerization NPArC # 16499153
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Share It Binding of human angiogenin inhibits actin polymerization NPArC # 16499153
 
4. Structure dissection of human progranulin identifies well-folded granulin/epithelin modules with unique functional activities NPArC # 3540169  
Search for Tolkatchev, Dmitri; Search for Malik, Suneil; Search for Vinogradova, Anna; Search for Wang, Ping; Search for Chen, Zhigang; Search for Xu, Ping; Search for Bennett, Hugh P. J.; Search for Bateman, Andrew; Search for Ni, Feng
Protein Sci, 17 (4), 2008, p. 711-724
Resolve DOI: http://dx.doi.org/10.1110/ps.073295308
Find@CISTI Structure dissection of human progranulin identifies well-folded granulin/epithelin modules with unique functional activities NPArC # 3540169 (Opens in a new window)Find@CISTI Structure dissection of human progranulin identifies well-folded granulin/epithelin modules with unique functional activities NPArC # 3540169
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Share It Structure dissection of human progranulin identifies well-folded granulin/epithelin modules with unique functional activities NPArC # 3540169
 
5. Conformational analyses of a partially-folded bioactive prodomain of human furin NPArC # 3538716  
Search for Bhattacharjya, Surajit; Search for Xu, Ping; Search for Wang, Ping; Search for Osborne, Michael J.; Search for Ni, Feng
86 (4), 2007, p. 329-344
Resolve DOI: http://dx.doi.org/10.1002/bip.20748
Find@CISTI Conformational analyses of a partially-folded bioactive prodomain of human furin NPArC # 3538716 (Opens in a new window)Find@CISTI Conformational analyses of a partially-folded bioactive prodomain of human furin NPArC # 3538716
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Share It Conformational analyses of a partially-folded bioactive prodomain of human furin NPArC # 3538716
 
6. Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni NPArC # 3539880  
Search for Tolkatchev, Dmitri; Search for Shaykhutdinov, Rustem; Search for Xu, Ping; Search for Plamondon, Josée; Search for Watson, David C.; Search for Young, Martin; Search for Ni, Feng
15 (10), 2006, p. 2381-2394
Find@CISTI Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni NPArC # 3539880 (Opens in a new window)Find@CISTI Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni NPArC # 3539880
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Share It Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni NPArC # 3539880
 
7. Isolation of monomeric human VHS by a phage selection NPArC # 3539892  
Search for To, Rebecca; Search for Hirama, Tomoko; Search for Arbabi-Ghahroudi, Mehdi; Search for MacKenzie, Roger; Search for Wang, Ping; Search for Xu, Ping; Search for Ni, Feng; Search for Tanha, Jamshid
The Journal of Biological Chemistry, 280 (50), 2005-12-16, p. 41395-41403
Resolve DOI: http://dx.doi.org/10.1074/jbc.M509900200
Find@CISTI Isolation of monomeric human VHS by a phage selection NPArC # 3539892 (Opens in a new window)Find@CISTI Isolation of monomeric human VHS by a phage selection NPArC # 3539892
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Share It Isolation of monomeric human VHS by a phage selection NPArC # 3539892
 
8. A Bivalent Dissectional Analysis of the High-Affinity Interactions between Cdc42 and the Cdc42/Rac Interactive Binding Domains of Signaling Kinases in Candida albicans NPArC # 3538610  
Search for Su, Zhengding; Search for Osborne, Michael J.; Search for Xu, Ping; Search for Xu, Xiaolong; Search for Li, Yang; Search for Ni, Feng
44 (50), 2005, p. 16461-16474
Resolve DOI: http://dx.doi.org/10.1021/bi050846l
Find@CISTI A Bivalent Dissectional Analysis of the High-Affinity Interactions between Cdc42 and the Cdc42/Rac Interactive Binding Domains of Signaling Kinases in Candida albicans NPArC # 3538610 (Opens in a new window)Find@CISTI A Bivalent Dissectional Analysis of the High-Affinity Interactions between Cdc42 and the Cdc42/Rac Interactive Binding Domains of Signaling Kinases in Candida albicans NPArC # 3538610
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Share It A Bivalent Dissectional Analysis of the High-Affinity Interactions between Cdc42 and the Cdc42/Rac Interactive Binding Domains of Signaling Kinases in Candida albicans NPArC # 3538610
 
9. Solution structure of the ligand binding domain of the fibroblast growth factor receptor : Role of heparin in the activation of the receptor NPArC # 3539795  
Search for Hung, Kuo-Wei; Search for Kumar, Thallapuranam Krishnaswamy S.; Search for Kathir, Karuppanan Muthusamy; Search for Xu, Ping; Search for Ni, Feng; Search for Ji, Hsiang-Hui; Search for Chen, Mei-Chi; Search for Yang, Chu-Chi; Search for Lin, Fu-Pang; Search for Chiu, Ing-Ming; Search for Yu, Chin
Biochemistry, 44 (48), 2005, p. 15787-15798
Resolve DOI: http://dx.doi.org/10.1021/bi051030n
Find@CISTI Solution structure of the ligand binding domain of the fibroblast growth factor receptor : Role of heparin in the activation of the receptor NPArC # 3539795 (Opens in a new window)Find@CISTI Solution structure of the ligand binding domain of the fibroblast growth factor receptor : Role of heparin in the activation of the receptor NPArC # 3539795
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Share It Solution structure of the ligand binding domain of the fibroblast growth factor receptor : Role of heparin in the activation of the receptor NPArC # 3539795
 
10. Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast : implications for efficient signaling through the MAPK cascades NPArC # 12326988  
Search for Bhattacharjya, Surajit; Search for Xu, Ping; Search for Chakrapani, Mukundan; Search for Johnston, Linda; Search for Ni, Feng
Protein Science, 14 (3), 2005-03, p. 828-835
Resolve DOI: http://dx.doi.org/10.1110/ps.041122105
Find@CISTI Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast : implications for efficient signaling through the MAPK cascades NPArC # 12326988 (Opens in a new window)Find@CISTI Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast : implications for efficient signaling through the MAPK cascades NPArC # 12326988
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Share It Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast : implications for efficient signaling through the MAPK cascades NPArC # 12326988
 
11. Solution Structure of the Dimeric SAM Domain of MAPKK Ste11 and its interactions with the Adaptor Protein Ste50 from the Budding Yeast: Implications for Ste11 Activation and Signal Transmission Through the Ste50-Ste11 Complex NPArC # 3538865  
Search for Bhattacharjya, Surajit; Search for Xu, Ping; Search for Gingras, Richard; Search for Shaykhutdinov, Rustem; Search for Wu, Cunle; Search for Whiteway, Malcolm; Search for Ni, Feng
J Mol Biol, 344, 2004, p. 1071-1087
Resolve DOI: http://dx.doi.org/10.1016/j.jmb.2004.09.018
Find@CISTI Solution Structure of the Dimeric SAM Domain of MAPKK Ste11 and its interactions with the Adaptor Protein Ste50 from the Budding Yeast: Implications for Ste11 Activation and Signal Transmission Through the Ste50-Ste11 Complex NPArC # 3538865 (Opens in a new window)Find@CISTI Solution Structure of the Dimeric SAM Domain of MAPKK Ste11 and its interactions with the Adaptor Protein Ste50 from the Budding Yeast: Implications for Ste11 Activation and Signal Transmission Through the Ste50-Ste11 Complex NPArC # 3538865
 | 
Share It Solution Structure of the Dimeric SAM Domain of MAPKK Ste11 and its interactions with the Adaptor Protein Ste50 from the Budding Yeast: Implications for Ste11 Activation and Signal Transmission Through the Ste50-Ste11 Complex NPArC # 3538865
 
12. HCV NS5B polymerase-bound conformation of a soluble sulfonamide inhibitor by 2D tranferred NOESY NPArC # 3539714  
Search for Yannopoulos, Constantin G.; Search for Xu, Ping; Search for Ni, Feng; Search for Chan, Laval; Search for Pereira, Oswy Z.; Search for Reddy, T. Jagadeeswar; Search for Das, Sanjoy K.; Search for Poisson, Carl; Search for Nguyen-Ba, Nghe; Search for Turcotte, Nathalie; Search for Proulx, Melanie; Search for Halab, Lilanne; Search for Wang, Wuyi; Search for Bédard, Jean; Search for Morin, Nicolas; Search for Hamel, Martine; Search for Nicolas, Olivier; Search for Bilimoria, Darious; Search for L'Heureux, Lucille; Search for Bethel, Richard; Search for Dionne, Gervais
Bioorganic & Medicinal Chemistry Letters, 14 (21), 2004, p. 5333-5337
Resolve DOI: http://dx.doi.org/10.1016/j.bmcl.2004.08.018
Find@CISTI HCV NS5B polymerase-bound conformation of a soluble sulfonamide inhibitor by 2D tranferred NOESY NPArC # 3539714 (Opens in a new window)Find@CISTI HCV NS5B polymerase-bound conformation of a soluble sulfonamide inhibitor by 2D tranferred NOESY NPArC # 3539714
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Share It HCV NS5B polymerase-bound conformation of a soluble sulfonamide inhibitor by 2D tranferred NOESY NPArC # 3539714
 
13. Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein NPArC # 3539045  
Search for Su, Zhengding; Search for Xu, Ping; Search for Ni, Feng
271 (9), 2004, p. 1725-1736
Resolve DOI: http://dx.doi.org/10.1111/j.1432-1033.2004.04078.x
Find@CISTI Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein NPArC # 3539045 (Opens in a new window)Find@CISTI Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein NPArC # 3539045
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Share It Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein NPArC # 3539045
 
14. Probing the Kinetic Landscape of Transient Peptide-Protein Interactions by Use of Peptide NMR Relaxation Dispersion Spectroscopy: Binding of an Antithrombin Peptide to Human Prothrombin NPArC # 3540051  
Search for Tolkatchev, Dmitri; Search for Xu, Ping; Search for Ni, Feng
125, 2003, p. 12432-12442
Resolve DOI: http://dx.doi.org/10.1021/ja021238l
Find@CISTI Probing the Kinetic Landscape of Transient Peptide-Protein Interactions by Use of Peptide NMR Relaxation Dispersion Spectroscopy: Binding of an Antithrombin Peptide to Human Prothrombin NPArC # 3540051 (Opens in a new window)Find@CISTI Probing the Kinetic Landscape of Transient Peptide-Protein Interactions by Use of Peptide NMR Relaxation Dispersion Spectroscopy: Binding of an Antithrombin Peptide to Human Prothrombin NPArC # 3540051
 | 
Share It Probing the Kinetic Landscape of Transient Peptide-Protein Interactions by Use of Peptide NMR Relaxation Dispersion Spectroscopy: Binding of an Antithrombin Peptide to Human Prothrombin NPArC # 3540051
 
15. Solution Structure and Backbone Dynamics of the Functional Cytoplasmic Subdomain of Human Ephrin B2, a Cell-Surface Ligand with Bidirectional Signaling Properties NPArC # 3539812  
Search for Song, Jianxing; Search for Vranken, Wim; Search for Xu, Ping; Search for Gingras, Richard; Search for Noyce, Ryan S.; Search for Yu, Zhenbao; Search for Shen, Shi-Hsiang; Search for Ni, Feng
41 (36), 2002, p. 10942-10949
Resolve DOI: http://dx.doi.org/10.1021/bi025815u
Find@CISTI Solution Structure and Backbone Dynamics of the Functional Cytoplasmic Subdomain of Human Ephrin B2, a Cell-Surface Ligand with Bidirectional Signaling Properties NPArC # 3539812 (Opens in a new window)Find@CISTI Solution Structure and Backbone Dynamics of the Functional Cytoplasmic Subdomain of Human Ephrin B2, a Cell-Surface Ligand with Bidirectional Signaling Properties NPArC # 3539812
 | 
Share It Solution Structure and Backbone Dynamics of the Functional Cytoplasmic Subdomain of Human Ephrin B2, a Cell-Surface Ligand with Bidirectional Signaling Properties NPArC # 3539812
 
16. Stability of Protein-Bound Conformations of Bioactive Peptides: The Folded Conformation of an Epidermal Growth Factor-Like Thrombomodulin Fragment is Similar to that Recognize by Thrombin NPArC # 3539543  
Search for Song, Jianxing; Search for Xu, Ping; Search for Koutychenko, Anatol; Search for Ni, Feng
65 (6), 2002, p. 373-386
Resolve DOI: http://dx.doi.org/10.1002/bip.10253
Find@CISTI Stability of Protein-Bound Conformations of Bioactive Peptides: The Folded Conformation of an Epidermal Growth Factor-Like Thrombomodulin Fragment is Similar to that Recognize by Thrombin NPArC # 3539543 (Opens in a new window)Find@CISTI Stability of Protein-Bound Conformations of Bioactive Peptides: The Folded Conformation of an Epidermal Growth Factor-Like Thrombomodulin Fragment is Similar to that Recognize by Thrombin NPArC # 3539543
 | 
Share It Stability of Protein-Bound Conformations of Bioactive Peptides: The Folded Conformation of an Epidermal Growth Factor-Like Thrombomodulin Fragment is Similar to that Recognize by Thrombin NPArC # 3539543
 
17. Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface NPArC # 3539104  
Search for Vranken, Wim; Search for Tolkatchev, Dmitri; Search for Xu, Ping; Search for Tanha, Jamshid; Search for Chen, Zhigang; Search for Narang, Saran; Search for Ni, Feng
Biochemistry, 41 (27), 2002-06-11, p. 8570-8579
Resolve DOI: http://dx.doi.org/10.1021/bi012169a
Find@CISTI Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface NPArC # 3539104 (Opens in a new window)Find@CISTI Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface NPArC # 3539104
 | 
Share It Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface NPArC # 3539104
 
18. pH-Induced conformational transitions of a molten-globule-like state of the inhibitory prodomain of furin: Implications for zymogen activation NPArC # 3540034  
Search for Bhattacharjya, Surajit; Search for Xu, Ping; Search for Xiang, Hui; Search for Chretien, Michel; Search for Seidah, Nabil G.; Search for Ni, Feng
Protein Science, 10 (5), 2001, p. 934-942
Find@CISTI pH-Induced conformational transitions of a molten-globule-like state of the inhibitory prodomain of furin: Implications for zymogen activation NPArC # 3540034 (Opens in a new window)Find@CISTI pH-Induced conformational transitions of a molten-globule-like state of the inhibitory prodomain of furin: Implications for zymogen activation NPArC # 3540034
 | 
Share It pH-Induced conformational transitions of a molten-globule-like state of the inhibitory prodomain of furin: Implications for zymogen activation NPArC # 3540034
 
19. Optimal design features of camelized human single-domain antibody libraries NPArC # 3539967  
Search for Tanha, Jamshid; Search for Xu, Ping; Search for Chen, Zhigang; Search for Ni, Feng; Search for Kaplan, Howard; Search for Narang, Saran A.; Search for MacKenzie, C. Roger
Journal of Biological Chemistry, 276 (27), 2001-05-02, p. 24774-24780
Resolve DOI: http://dx.doi.org/10.1074/jbc.M100770200
Find@CISTI Optimal design features of camelized human single-domain antibody libraries NPArC # 3539967 (Opens in a new window)Find@CISTI Optimal design features of camelized human single-domain antibody libraries NPArC # 3539967
 | 
Share It Optimal design features of camelized human single-domain antibody libraries NPArC # 3539967
 
20. Molecular interactions of the Gbeta binding domain of the Ste20p/PAK family of protein kinases. An isolated but fully functional Gbeta binding domain from Ste20p is only partially folded as shown by heteronuclear NMR spectroscopy NPArC # 3539260  
Search for Song, Jianxing; Search for Chen, Zhigang; Search for Xu, Ping; Search for Gingras, Richard; Search for Ng, Andy; Search for Leberer, Ekkehard; Search for Thomas, David Y.; Search for Ni, Feng
276 (44), 2001, p. 41205-41212
Resolve DOI: http://dx.doi.org/10.1074/jbc.M103449200
Find@CISTI Molecular interactions of the Gbeta binding domain of the Ste20p/PAK family of protein kinases. An isolated but fully functional Gbeta binding domain from Ste20p is only partially folded as shown by heteronuclear NMR spectroscopy NPArC # 3539260 (Opens in a new window)Find@CISTI Molecular interactions of the Gbeta binding domain of the Ste20p/PAK family of protein kinases. An isolated but fully functional Gbeta binding domain from Ste20p is only partially folded as shown by heteronuclear NMR spectroscopy NPArC # 3539260
 | 
Share It Molecular interactions of the Gbeta binding domain of the Ste20p/PAK family of protein kinases. An isolated but fully functional Gbeta binding domain from Ste20p is only partially folded as shown by heteronuclear NMR spectroscopy NPArC # 3539260
 
21. Letter to the Editor: Sequence-specific 1H, 15N and 13C resonance assignments of the inhibitory prodomain of human furin NPArC # 3539734  
Search for Bhattacharjya, Surajit; Search for Xu, Ping; Search for Ni, Feng
16 (3), 2000, p. 275-276
Resolve DOI: http://dx.doi.org/10.1023/A:1008323817091
Find@CISTI Letter to the Editor: Sequence-specific 1H, 15N and 13C resonance assignments of the inhibitory prodomain of human furin NPArC # 3539734 (Opens in a new window)Find@CISTI Letter to the Editor: Sequence-specific 1H, 15N and 13C resonance assignments of the inhibitory prodomain of human furin NPArC # 3539734
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Share It Letter to the Editor: Sequence-specific 1H, 15N and 13C resonance assignments of the inhibitory prodomain of human furin NPArC # 3539734
 
22. Solution structure of the osteogenic 1-31 fragment of the human parathyroid hormone NPArC # 3539811  
Search for Chen, Zhigang; Search for Xu, Ping; Search for Barbier, Jean-René; Search for Willick, Gordon; Search for Ni, Feng
39 (42), 2000, p. 12766-12777
Resolve DOI: http://dx.doi.org/10.1021/bi000882e
Find@CISTI Solution structure of the osteogenic 1-31 fragment of the human parathyroid hormone NPArC # 3539811 (Opens in a new window)Find@CISTI Solution structure of the osteogenic 1-31 fragment of the human parathyroid hormone NPArC # 3539811
 | 
Share It Solution structure of the osteogenic 1-31 fragment of the human parathyroid hormone NPArC # 3539811
 
23. Inhibitory activity and structural characterization of a C-terminal peptide fragment derived from the prosegment of the proprotein convertase PC7 NPArC # 3539655  
Search for Bhattacharjya, Surajit; Search for Xu, Ping; Search for Zhong, Mei; Search for Chretien, Michel; Search for Seidah, Nabil G.; Search for Ni, Feng
39 (11), 2000, p. 2868-2877
Resolve DOI: http://dx.doi.org/10.1021/bi9923961
Find@CISTI Inhibitory activity and structural characterization of a C-terminal peptide fragment derived from the prosegment of the proprotein convertase PC7 NPArC # 3539655 (Opens in a new window)Find@CISTI Inhibitory activity and structural characterization of a C-terminal peptide fragment derived from the prosegment of the proprotein convertase PC7 NPArC # 3539655
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Share It Inhibitory activity and structural characterization of a C-terminal peptide fragment derived from the prosegment of the proprotein convertase PC7 NPArC # 3539655
 
24. The active-site residue Cys-29 is responsible for the neutral-pH inactivation and the refolding barrier of human cathepsin B NPArC # 3539423  
Search for Song, Jianxing; Search for Xu, Ping; Search for Xiang, Hui; Search for Su, Zhengding; Search for Storer, Andrew C.; Search for Ni, Feng
FEBS Letters, 475 (3), 2000, p. 157-162
Resolve DOI: http://dx.doi.org/10.1016/S0014-5793(00)01644-6
Find@CISTI The active-site residue Cys-29 is responsible for the neutral-pH inactivation and the refolding barrier of human cathepsin B NPArC # 3539423 (Opens in a new window)Find@CISTI The active-site residue Cys-29 is responsible for the neutral-pH inactivation and the refolding barrier of human cathepsin B NPArC # 3539423
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Share It The active-site residue Cys-29 is responsible for the neutral-pH inactivation and the refolding barrier of human cathepsin B NPArC # 3539423
 
25. Transferred C-13 T-1 relaxation at natural isotopic abundance: A practical method for determining site-specific changes in ligand flexibility upon binding to a macromolecule NPArC # 3540236  
Search for LaPlante, Steven R.; Search for Aubry, Norman; Search for Deziel, Robert; Search for Ni, Feng; Search for Xu, Ping
Journal of the American Chemical Society, 122 (50), 2000, p. 12530-12535
Resolve DOI: http://dx.doi.org/10.1021/ja0017817
Find@CISTI Transferred C-13 T-1 relaxation at natural isotopic abundance: A practical method for determining site-specific changes in ligand flexibility upon binding to a macromolecule NPArC # 3540236 (Opens in a new window)Find@CISTI Transferred C-13 T-1 relaxation at natural isotopic abundance: A practical method for determining site-specific changes in ligand flexibility upon binding to a macromolecule NPArC # 3540236
 | 
Share It Transferred C-13 T-1 relaxation at natural isotopic abundance: A practical method for determining site-specific changes in ligand flexibility upon binding to a macromolecule NPArC # 3540236
 
 
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