Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors |
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30977 | 2022-05-26 | Chemical Shifts: 1 set |
NMR structure of crosslinked cyclophilin A |
The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink
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A M Gronenborn, C D Schwieters, D Toptygin, E C Lipinski, I JL Byeon, J Ahn, M Lu, Y Shi, Y Xiang |
30942 | 2022-07-13 | Chemical Shifts: 1 set |
An RNA aptamer that decreases flavin redox potential |
An RNA aptamer that shifts the reduction potential of metabolic cofactors
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Dana A Baum, Donald H Burke, Johan A Carballo, John S Samuelian, Jun Li, Manami Roychowdhury-Saha, Raghav R Poudyal, Seth A Staller, Shi-Jie Chen, Thomas J Gremminger, Xiao Heng, Yuanzhe Zhou, Zhenwei Song |
30868 | 2021-03-12 | Chemical Shifts: 1 set |
Solution structure of the HIV-1 PBS-segment |
The three-way junction structure of the HIV-1 PBS-segment binds host enzyme important for viral infectivity
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Gatikrushna Singh, Juan Ji, Jun Li, Kathleen Boris-Lawrie, Liming Qiu, Margaret J Lange, Shi-Jie J Chen, Thomas Gremminger, Xiaobing Zuo, Xiao Heng, Xiaoqin Zou, Yi Cheng, Zhenwei Song |
30788 | 2020-10-05 | Chemical Shifts: 1 set |
The FARFAR-NMR Ensemble of 29-mer HIV-1 Trans-activation Response Element RNA (N=20) |
Rapid and accurate determination of atomistic RNA dynamic ensemble models using NMR and structure prediction
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A Rangadurai, D A Case, D Herschlag, H Abou-Assi, H M Al-Hashimi, H Shi, J D Yesselman, R Roy |
30714 | 2020-07-05 | Chemical Shifts: 1 set |
Solution NMR structure of Prochlorosin 2.1 produced by Prochlorococcus MIT 9313 |
Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria.
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B Li, D Rusch, D Sher, I Joewono, K Huang, L Kelly, P J Knerr, S W Chisholm, W A van der Donk, Y Shi |
30713 | 2020-07-05 | Chemical Shifts: 1 set |
Solution NMR structure of Prochlorosin 2.10 produced by Prochlorococcus MIT 9313 |
Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria.
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B Li, D Rusch, D Sher, I Joewono, K Huang, L Kelly, P J Knerr, S W Chisholm, W A van der Donk, Y Shi |
30585 | 2019-05-17 | Chemical Shifts: 1 set |
Solution structure of MLL4 PHD6 domain in complex with histone H4K16ac peptide |
Selective binding of the PHD6 finger of MLL4 to histone H4K16ac links MLL4 and MOF
|
B D Strahl, B J Klein, E M Cornett, J E Lee, J W Ahn, K Ge, K Krajewski, L Xu, M R Holden, R G Roeder, S B Rothbart, S P Wang, T G Kutateladze, X Shi, Y Dou, Y Jang, Y Zhang |
30517 | 2020-02-28 | Chemical Shifts: 1 set |
Solution NMR structure of the KCNQ1 voltage-sensing domain |
Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state
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A L George, C R Sanders, D Peng, G Kuenze, H Huang, J A Smith, J Cui, J Meiler, J Shi, K C Taylor, K M White, N Yang, P Hou, P W Kang, R L McFeeters |
30413 | 2018-05-10 | Chemical Shifts: 1 set |
JzTx-V toxin peptide, wild-type |
Pharmacological characterization of potent and selective NaV1.7 inhibitors engineered from Chilobrachys jingzhao tarantula venom peptide JzTx-V.
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A Zou, B D Moyer, B Wu, D Liu, J B Jordan, J H Lee, J K Murray, J Ligutti, J Long, K Andrews, K Biswas, K Sham, L P Miranda, L Shi, P Favreau, R Stocklin, R Yin, V Yu |
30411 | 2018-04-30 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
Solution NMR structure of JzTx-V, a Nav 1.7 inhibitory peptide |
Pharmacological characterization of potent and selective NaV1.7 inhibitors engineered from Chilobrachys jingzhao tarantula venom peptide JzTx-V.
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A Zou, B D Moyer, B Wu, D Liu, J B Jordan, J H Lee, J K Murray, J Ligutti, J Long, K Andrews, K Biswas, K Sham, L Miranda, L Shi, P Favreau, R Stocklin, R Yin, V Yu |
36117 | 2018-02-06 | Chemical Shifts: 1 set |
SOLUTION STRUCTURE OF HUMAN MOG1 |
Mitosis-specific acetylation tunes Ran effector binding for chromosome segregation
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H Liu, J Wu, J Zhang, K Ruan, Q Gong, Q Hu, R Tian, S Akram, W Wang, X Bao, X Liu, X Yao, X Yuan, Y Liu, Y Shi, Y Zhang, Z Dou, Z Zhang |
34167 | 2017-09-29 | Chemical Shifts: 1 set Spectral_peak_list: 3 sets |
Solution structure of domain III (DIII)of Zika virus Envelope protein |
A Human Bi-specific Antibody against Zika Virus with High Therapeutic Potential.
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A Cavalli, A Lanzavecchia, A Rubio, D A Espinosa, D Corti, E Cameroni, E Harris, E Vicenzi, E XY Lim, F Sallusto, F Zatta, G Fibriansah, I Pagani, J Shi, J Wang, K Stettler, L Simonelli, L Varani, M Bardelli, M Beltramello, M Foglierini, M Pedotti, O Zerbe, R Hewson, S Bianchi, S Dowall, S Jaconi, S Jurt, S M Lok, S Pullan, T Barca, T S Ng, V Broccoli, V Graham |
30177 | 2016-10-07 | Chemical Shifts: 1 set |
Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide |
PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation
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Brianna J Klein, Chao Yuan, Christiane J Bruns, Gaofeng Cui, Georges Mer, Kevin Lin, Maria Victoria V Botuyan, Tatiana G Kutateladze, Xiaobing Shi, Xiaolu Wang, Xiaoyan Wang, Yue Lu, Yue Zhao |
25995 | 2016-07-18 | Chemical Shifts: 1 set |
Protein complex |
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome
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Hideki Aihara, Ke Shi, Kylie J Walters, Leah Randles, Sergey G Tarasov, Xiang Chen |
25657 | 2016-02-22 | Chemical Shifts: 1 set |
Proteasome protein fragment |
Structures of Rpn1:ubiquitin and Rpn1:K48 diubiquitin define Rpn1 as a novel proteasome ubiquitin receptor.
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Daniel Finley, Jacob Vannoy, Kylie J Walters, Sergey G Tarasov, Suzanne Elsasser, Xiang Chen, Yanhong Shi, Yuan Shi |
25527 | 2015-06-01 | Chemical Shifts: 1 set |
Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5 |
A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis
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Andrew J Borst, Daniel R Southworth, David Baker, Eric Tse, Katja D Dove, Lei Shi, Ponni Rajagopal, Rachel E Klevit, Scott P Delbecq |
15377 | 2008-03-13 | Chemical Shifts: 1 set |
Solution structure of human DESR1 |
Solution structure of human DESR1, a CSL zinc-binding protein.
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Fangming Wu, F Yang, H Huang, J Sun, J Wu, J Zhang, M Yu, P Ji, W Chu, Y Shi, Z Wu |
15150 | 2007-10-24 | Chemical Shifts: 1 set |
Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2 |
Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins
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D Xie, G Zhang, H Huang, J H Wu, J H Zhang, J W Wu, M Wu, P Ji, P Jiang, W Du, Y S Yang, Y Y Shi |
15129 | 2007-05-21 | Chemical Shifts: 1 set |
Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin |
Solution structure of the first SH3 domain of human Vinexin and its interaction with the vinculin peptides
|
B Yao, J Wu, J Zhang, Y Shi |
15057 | 2008-06-24 | Chemical Shifts: 1 set |
Solution Structrue of C-terminal Bromodomain of Brd4 |
Structural basis and binding properties of the second bromodomain of Brd4 with acetylated histone tails
|
B Ding, H Huang, J Wu, J Zhang, X Wang, Y Liu, Y Shi |
6473 | 2005-02-17 | Chemical Shifts: 1 set |
Structural and dynamic characteristics of the acid-unfolded state of hUBF HMG Box 1 provide clues for the early events in protien folding |
Compact molten globule-like state of hUBF HMG Box1 at extremely low pH
|
H Huang, Jiahai Zhang, Jihui Wu, J Xu, Q Chen, X Li, Xuecheng Zhang, Yunyu Shi |
6152 | 2004-05-15 | Chemical Shifts: 1 set |
Solution structure of TIP-B1 |
Solution structure of recombinant TIP-B1, a novel TNF inhibitory protein
|
C Xu, J H Wu, P C Zheng, Q H Zhang, Y J Tang, Y Q Xu, Y Y Shi, Y Z Du |
6037 | 2005-02-21 | Chemical Shifts: 1 set |
Solution Structure of BmKX, a novel potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch |
A novel short-chain peptide BmKX from the chinese scorpion Buthus martensi karsch, sequencing, gene cloning and structure determination
|
C G Wang, C-W Chi, J Wu, W Lu, Y Shi, Y Xu, Z Cai |
5392 | 2003-12-08 | Chemical Shifts: 1 set |
Solution structure of HMG box 5 in human upstream binding factor |
Solution structure and DNA binding property of the fifth HMG box domain in comparison with the first HMG box domain in human upstream binding factor
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J Wu, W Yang, W Zeng, Y Shi, Y Xu |
4585 | 2000-12-05 | Chemical Shifts: 1 set |
Solution Structure of BmP02, a new Potassium channel Blocker from the Venom of the Chinese Scorpion Buthus martensi Karsch |
Solution Structure of BmP02, a new Potassium channel Blocker from the Venom of the Chinese Scorpion Buthus martensi Karsch
|
J H Wu, J M Pei, Q C Tong, Y H Ji, Y Q Xu, Y Y Shi |
4124 | 1999-02-02 | Chemical Shifts: 1 set |
Main-chain Signal Assignment for the PDZ2 Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor |
Main-chain Signal Assignment for the PDZ2Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor
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Alex Koshy, Denis Banville, Irena Ekiel, Jacek J Slon-Usakiewicz, Kalle Gehring, Shi Hsiang Shen |
4123 | 1999-02-02 | Chemical Shifts: 1 set |
Main-chain Signal Assignment for the PDZ2 Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor |
Main-chain Signal Assignment for the PDZ2Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor
|
Alex Koshy, Denis Banville, Irena Ekiel, Jacek J Slon-Usakiewicz, Kalle Gehring, Shi Hsiang Shen |
1783 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1781 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1797 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1777 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1775 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1779 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1795 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1793 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1791 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1789 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1787 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1785 | 1995-07-31 | Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |