-
2
-
-
24644501099
-
Direct NMR observation of a substrate protein bound to the chaperonin GroEL
-
R. Horst, E.B. Bertelsen, J. Fiaux, G. Wider, A.L. Horwich, and K. Wuthrich Direct NMR observation of a substrate protein bound to the chaperonin GroEL Proc Natl Acad Sci USA 102 2005 12748 12753 The 20 kDa substrate protein human dihydrofolate reductase (DHFR) bound to the 800 kDa chaperonin GroEL or the 400 kDa single-ring analog, SR1, was directly analyzed with TROSY and CRINEPT experiments. This paper demonstrates that NMR is able to get unique structural and dynamic information on a system as large as 1 MDa.
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 12748-12753
-
-
Horst, R.1
Bertelsen, E.B.2
Fiaux, J.3
Wider, G.4
Horwich, A.L.5
Wuthrich, K.6
-
3
-
-
0038455923
-
NMR analysis of methyl groups at 100-500 kDa: Model systems and Arp2/3 complex
-
M. Kreishman-Deitrick, C. Egile, D.W. Hoyt, J.J. Ford, R. Li, and M.K. Rosen NMR analysis of methyl groups at 100-500 kDa: model systems and Arp2/3 complex Biochemistry 42 2003 8579 8586
-
(2003)
Biochemistry
, vol.42
, pp. 8579-8586
-
-
Kreishman-Deitrick, M.1
Egile, C.2
Hoyt, D.W.3
Ford, J.J.4
Li, R.5
Rosen, M.K.6
-
4
-
-
0037189901
-
Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase G
-
V. Tugarinov, R. Muhandiram, A. Ayed, and L.E. Kay Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase G J Am Chem Soc 124 2002 10025 10035
-
(2002)
J Am Chem Soc
, vol.124
, pp. 10025-10035
-
-
Tugarinov, V.1
Muhandiram, R.2
Ayed, A.3
Kay, L.E.4
-
5
-
-
1242308875
-
An isotope labeling strategy for methyl TROSY spectroscopy
-
V. Tugarinov, and L.E. Kay An isotope labeling strategy for methyl TROSY spectroscopy J Biomol NMR 28 2004 165 172
-
(2004)
J Biomol NMR
, vol.28
, pp. 165-172
-
-
Tugarinov, V.1
Kay, L.E.2
-
6
-
-
14144254537
-
Solution NMR-derived global fold of a monomeric 82-kDa enzyme
-
V. Tugarinov, W-Y. Choy, V.Y. Orekhov, and L.E. Kay Solution NMR-derived global fold of a monomeric 82-kDa enzyme Proc Natl Acad Sci USA 102 2005 622 627 The global folding of a monomeric 723-residue (82 kDa) enzyme, malate synthase G, was determined solely using NMR-derived constraints. This is the largest NMR protein structure solved so far. Deuteration with methyl labeling techniques and 4D pulse sequences were critical to solving this structure.
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 622-627
-
-
Tugarinov, V.1
Choy, W.-Y.2
Orekhov, V.Y.3
Kay, L.E.4
-
7
-
-
0141987859
-
Exchange-transferred NOE spectroscopy and bound ligand structure determination
-
C.B. Post Exchange-transferred NOE spectroscopy and bound ligand structure determination Curr Opin Struct Biol 13 2003 581 588
-
(2003)
Curr Opin Struct Biol
, vol.13
, pp. 581-588
-
-
Post, C.B.1
-
8
-
-
0033553844
-
Characterization of ligand binding by saturation transfer difference NMR spectroscopy
-
B.M. Moriz Mayer Characterization of ligand binding by saturation transfer difference NMR spectroscopy Angew Chem Int Ed 38 1999 1784 1788
-
(1999)
Angew Chem Int Ed
, vol.38
, pp. 1784-1788
-
-
Moriz Mayer, B.M.1
-
10
-
-
12444289530
-
3 in native platelets than in liposomes
-
3 molecules are estimated to be expressed on the surface of a single platelet, which corresponds to a 350 pmol protein concentration in the NMR sample. This example demonstrates the high sensitivity of STD NMR.
-
(2005)
J Am Chem Soc
, vol.127
, pp. 916-919
-
-
Claasen, B.1
Axmann, M.2
Meinecke, R.3
Meyer, B.4
-
11
-
-
0034823890
-
Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
-
M. Mayer, and B. Meyer Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor J Am Chem Soc 123 2001 6108 6117
-
(2001)
J Am Chem Soc
, vol.123
, pp. 6108-6117
-
-
Mayer, M.1
Meyer, B.2
-
12
-
-
26444514377
-
Determination of the conformation of trimethoprim in the binding pocket of bovine dihydrofolate reductase from a STD-NMR intensity-restrained CORCEMA-ST optimization
-
V. Jayalakshmi, and N.R. Krishna Determination of the conformation of trimethoprim in the binding pocket of bovine dihydrofolate reductase from a STD-NMR intensity-restrained CORCEMA-ST optimization J Am Chem Soc 127 2005 14080 14084 The structure of the complex between bovine DHFR and the antibacterial agent trimethoprim (TMP) was determined using SICO (STD-NMR intensity restrained complete relaxation) and conformational exchange matrix-saturation transfer (CORSEMA-ST) optimization. The analysis used the crystal coordinates of inhibitor-free bovine DHFR. The structure was essentially identical to the X-ray structure of the homologous chicken liver DHFR-TMP complex.
-
(2005)
J Am Chem Soc
, vol.127
, pp. 14080-14084
-
-
Jayalakshmi, V.1
Krishna, N.R.2
-
13
-
-
3242685827
-
Refinement of the conformation of UDP-galactose bound to galactosyltransferase using the STD NMR intensity-restrained CORCEMA optimization
-
V. Jayalakshmi, T. Biet, T. Peters, and N.R. Krishna Refinement of the conformation of UDP-galactose bound to galactosyltransferase using the STD NMR intensity-restrained CORCEMA optimization J Am Chem Soc 126 2004 8610 8611
-
(2004)
J Am Chem Soc
, vol.126
, pp. 8610-8611
-
-
Jayalakshmi, V.1
Biet, T.2
Peters, T.3
Krishna, N.R.4
-
14
-
-
0036290185
-
Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes
-
V. Jayalakshmi, and N.R. Krishna Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes J Magn Reson 155 2002 106 118
-
(2002)
J Magn Reson
, vol.155
, pp. 106-118
-
-
Jayalakshmi, V.1
Krishna, N.R.2
-
15
-
-
0043032424
-
The effect of relaxation on the epitope mapping by saturation transfer difference NMR
-
J. Yan, A.D. Kline, H. Mo, M.J. Shapiro, and E.R. Zartler The effect of relaxation on the epitope mapping by saturation transfer difference NMR J Magn Reson 163 2003 270 276
-
(2003)
J Magn Reson
, vol.163
, pp. 270-276
-
-
Yan, J.1
Kline, A.D.2
Mo, H.3
Shapiro, M.J.4
Zartler, E.R.5
-
16
-
-
1542366711
-
SOS-NMR: A saturation transfer NMR-based method for determining the structures of protein-ligand complexes
-
P.J. Hajduk, J.C. Mack, E.T. Olejniczak, C. Park, P.J. Dandliker, and B.A. Beutel SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes J Am Chem Soc 126 2004 2390 2398 The experiment termed SOS-NMR uses the principles of STD NMR. However, it is performed with a ligand bound to a series of protein samples that are perdeuterated except for individual amino acid types, such as isoleucine, leucine, valine or methionine. The differential degrees of saturation transfer were interpreted as ambiguous NOEs to construct models using a docking program. This was illustrated for FKBP-2-(3′-pyridyl)-benzimidazole and MurA-uridine diphosphate N-acetylglucosamine complexes.
-
(2004)
J Am Chem Soc
, vol.126
, pp. 2390-2398
-
-
Hajduk, P.J.1
MacK, J.C.2
Olejniczak, E.T.3
Park, C.4
Dandliker, P.J.5
Beutel, B.A.6
-
17
-
-
0036302354
-
Determination of the interface of a large protein complex by transferred cross-saturation measurements
-
T. Nakanishi, M. Miyazawa, M. Sakakura, H. Terasawa, H. Takahashi, and I. Shimada Determination of the interface of a large protein complex by transferred cross-saturation measurements J Mol Biol 318 2002 245 249
-
(2002)
J Mol Biol
, vol.318
, pp. 245-249
-
-
Nakanishi, T.1
Miyazawa, M.2
Sakakura, M.3
Terasawa, H.4
Takahashi, H.5
Shimada, I.6
-
18
-
-
0034051065
-
A novel NMR method for determining the interfaces of large protein-protein complexes
-
H. Takahashi, T. Nakanishi, K. Kami, Y. Arata, and I. Shimada A novel NMR method for determining the interfaces of large protein-protein complexes Nat Struct Biol 7 2000 220 223
-
(2000)
Nat Struct Biol
, vol.7
, pp. 220-223
-
-
Takahashi, H.1
Nakanishi, T.2
Kami, K.3
Arata, Y.4
Shimada, I.5
-
19
-
-
0242458492
-
+ channel and agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method
-
+ channel and agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method Structure 11 2003 1381 1392
-
(2003)
Structure
, vol.11
, pp. 1381-1392
-
-
Takeuchi, K.1
Yokogawa, M.2
Matsuda, T.3
Sugai, M.4
Kawano, S.5
Kohno, T.6
Nakamura, H.7
Takahashi, H.8
Shimada, I.9
-
20
-
-
32344438018
-
Direct determination of a membrane-peptide interface using the nuclear magnetic resonance cross-saturation method
-
T. Nakamura, H. Takahashi, K. Takeuchi, T. Kohno, K. Wakamatsu, and I. Shimada Direct determination of a membrane-peptide interface using the nuclear magnetic resonance cross-saturation method Biophys J 105 2005 066910
-
(2005)
Biophys J
, vol.105
, pp. 066910
-
-
Nakamura, T.1
Takahashi, H.2
Takeuchi, K.3
Kohno, T.4
Wakamatsu, K.5
Shimada, I.6
-
21
-
-
0037222091
-
Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experiment
-
N. Nishida, H. Sumikawa, M. Sakakura, N. Shimba, H. Takahashi, H. Terasawa, E.I. Suzuki, and I. Shimada Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experiment Nat Struct Biol 10 2003 53 58
-
(2003)
Nat Struct Biol
, vol.10
, pp. 53-58
-
-
Nishida, N.1
Sumikawa, H.2
Sakakura, M.3
Shimba, N.4
Takahashi, H.5
Terasawa, H.6
Suzuki, E.I.7
Shimada, I.8
-
22
-
-
24144471856
-
Bead-linked proteoliposomes: A reconstitution method for NMR analyses of membrane protein-ligand interactions
-
M. Yokogawa, K. Takeuchi, and I. Shimada Bead-linked proteoliposomes: a reconstitution method for NMR analyses of membrane protein-ligand interactions J Am Chem Soc 127 2005 12021 12027 A new strategy for membrane protein reconstitution into lipid bilayers bound to affinity beads was established. The strategy was successfully applied to the interaction between a potassium ion channel, KcsA, and a pore blocker, agitoxin2 (AgTx2). The KcsA-binding site of AgTx2 was mapped using TCS. This strategy is useful for analyzing interactions with membrane proteins that need a lipid bilayer environment and are unstable in detergent micelles.
-
(2005)
J Am Chem Soc
, vol.127
, pp. 12021-12027
-
-
Yokogawa, M.1
Takeuchi, K.2
Shimada, I.3
-
23
-
-
0033610476
-
Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes
-
H. Matsuo, K.J. Walters, K. Teruya, T. Tanaka, G.T. Gassner, S.J. Lippard, Y. Kyogoku, and G. Wagner Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes J Am Chem Soc 121 1999 9903 9904
-
(1999)
J Am Chem Soc
, vol.121
, pp. 9903-9904
-
-
Matsuo, H.1
Walters, K.J.2
Teruya, K.3
Tanaka, T.4
Gassner, G.T.5
Lippard, S.J.6
Kyogoku, Y.7
Wagner, G.8
-
24
-
-
16344378243
-
Mapping the interaction surface of a membrane protein: Unveiling the conformational switch of phospholamban in calcium pump regulation
-
J. Zamoon, F. Nitu, C. Karim, D.D. Thomas, and G. Veglia Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation Proc Natl Acad Sci USA 102 2005 4747 4752 The binding site on phospholamban (PLN) for sarcoplasmic reticulum calcium ATPase (SERCA) (total molecular weight greater than 120 kDa) was successfully mapped in CHAPS micelles. This paper demonstrates the robustness of differential line broadening experiments for mapping binding sites between membrane proteins.
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 4747-4752
-
-
Zamoon, J.1
Nitu, F.2
Karim, C.3
Thomas, D.D.4
Veglia, G.5
-
25
-
-
0041989754
-
A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex
-
S.C. Panchal, D.A. Kaiser, E. Torres, T.D. Pollard, and M.K. Rosen A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex Nat Struct Biol 10 2003 591 598
-
(2003)
Nat Struct Biol
, vol.10
, pp. 591-598
-
-
Panchal, S.C.1
Kaiser, D.A.2
Torres, E.3
Pollard, T.D.4
Rosen, M.K.5
-
26
-
-
0242290223
-
Hyaluronan recognition mode of CD44 revealed by cross-saturation and chemical shift perturbation experiments
-
M. Takeda, H. Terasawa, M. Sakakura, Y. Yamaguchi, M. Kajiwara, H. Kawashima, M. Miyasaka, and I. Shimada Hyaluronan recognition mode of CD44 revealed by cross-saturation and chemical shift perturbation experiments J Biol Chem 278 2003 43550 43555
-
(2003)
J Biol Chem
, vol.278
, pp. 43550-43555
-
-
Takeda, M.1
Terasawa, H.2
Sakakura, M.3
Yamaguchi, Y.4
Kajiwara, M.5
Kawashima, H.6
Miyasaka, M.7
Shimada, I.8
-
27
-
-
22144435546
-
The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy
-
D.J. Hamel, and F.W. Dahlquist The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy J Am Chem Soc 127 2005 9676 9677 By comparing the resonance line widths of ligands in contact with either non-labeled or deuterated receptor protein, the authors mapped the CheW-binding site of CheA. The complex has a molecular mass of 120 kDa. Only the resonances from the interface sense the different proton densities of the receptor protein in the two samples and exhibit different degrees of line broadening, thus revealing the binding face.
-
(2005)
J Am Chem Soc
, vol.127
, pp. 9676-9677
-
-
Hamel, D.J.1
Dahlquist, F.W.2
-
28
-
-
0031000510
-
Direct measurement of angles between bond vectors in high-resolution NMR
-
B. Reif, M. Hennig, and C. Griesinger Direct measurement of angles between bond vectors in high-resolution NMR Science 276 1997 1230 1233
-
(1997)
Science
, vol.276
, pp. 1230-1233
-
-
Reif, B.1
Hennig, M.2
Griesinger, C.3
-
29
-
-
0037663864
-
Derivation of dihedral angles from CH-CH dipolar-dipolar cross-correlated relaxation rates: A C-C torsion involving a quaternary carbon atom in epothilone a bound to tubulin
-
T. Carlomagno, V.M. Sanchez, M.J. Blommers, and C. Griesinger Derivation of dihedral angles from CH-CH dipolar-dipolar cross-correlated relaxation rates: A C-C torsion involving a quaternary carbon atom in epothilone A bound to tubulin Angew Chem Int Ed Engl 42 2003 2515 2517
-
(2003)
Angew Chem Int Ed Engl
, vol.42
, pp. 2515-2517
-
-
Carlomagno, T.1
Sanchez, V.M.2
Blommers, M.J.3
Griesinger, C.4
-
30
-
-
0038339605
-
The high-resolution solution structure of epothilone a bound to tubulin: An understanding of the structure-activity relationships for a powerful class of antitumor agents
-
T. Carlomagno, M.J. Blommers, J. Meiler, W. Jahnke, T. Schupp, F. Petersen, D. Schinzer, K.H. Altmann, and C. Griesinger The high-resolution solution structure of epothilone A bound to tubulin: an understanding of the structure-activity relationships for a powerful class of antitumor agents Angew Chem Int Ed Engl 42 2003 2511 2515
-
(2003)
Angew Chem Int Ed Engl
, vol.42
, pp. 2511-2515
-
-
Carlomagno, T.1
Blommers, M.J.2
Meiler, J.3
Jahnke, W.4
Schupp, T.5
Petersen, F.6
Schinzer, D.7
Altmann, K.H.8
Griesinger, C.9
-
31
-
-
0025252231
-
Heteronuclear filters in two-dimensional [1H, 1H]-NMR spectroscopy: Combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions
-
G. Otting, and K. Wuthrich Heteronuclear filters in two-dimensional [1H, 1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions Q Rev Biophys 23 1990 39 96
-
(1990)
Q Rev Biophys
, vol.23
, pp. 39-96
-
-
Otting, G.1
Wuthrich, K.2
-
32
-
-
0000165109
-
Isotope-filtered 2D NMR of a protein-peptide complex: Study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin
-
M. Ikura, and A. Bax Isotope-filtered 2D NMR of a protein-peptide complex: study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin J Am Chem Soc 114 1992 2433 2440
-
(1992)
J Am Chem Soc
, vol.114
, pp. 2433-2440
-
-
Ikura, M.1
Bax, A.2
-
33
-
-
0034924193
-
Characterizing protein-protein complexes and oligomers by nuclear magnetic resonance spectroscopy
-
K.J. Walters, A.E. Ferentz, B.J. Hare, P. Hidalgo, A. Jasanoff, H. Matsuo, and G. Wagner Characterizing protein-protein complexes and oligomers by nuclear magnetic resonance spectroscopy Methods Enzymol 339 2001 238 258
-
(2001)
Methods Enzymol
, vol.339
, pp. 238-258
-
-
Walters, K.J.1
Ferentz, A.E.2
Hare, B.J.3
Hidalgo, P.4
Jasanoff, A.5
Matsuo, H.6
Wagner, G.7
-
34
-
-
0001050734
-
A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry
-
K.J. Walters, H. Matsuo, and G. Wagner A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry J Am Chem Soc 119 1997 5958 5959
-
(1997)
J Am Chem Soc
, vol.119
, pp. 5958-5959
-
-
Walters, K.J.1
Matsuo, H.2
Wagner, G.3
-
35
-
-
0347281686
-
Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E
-
J.D. Gross, N.J. Moerke, T. von der Haar, A.A. Lugovskoy, A.B. Sachs, J.E.G. McCarthy, and G. Wagner Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E Cell 115 2003 739 750
-
(2003)
Cell
, vol.115
, pp. 739-750
-
-
Gross, J.D.1
Moerke, N.J.2
Von Der Haar, T.3
Lugovskoy, A.A.4
Sachs, A.B.5
McCarthy, J.E.G.6
Wagner, G.7
-
36
-
-
0037354160
-
A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes
-
J.D. Gross, V.M. Gelev, and G. Wagner A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes J Biomol NMR 25 2003 235 242
-
(2003)
J Biomol NMR
, vol.25
, pp. 235-242
-
-
Gross, J.D.1
Gelev, V.M.2
Wagner, G.3
-
37
-
-
0034254909
-
Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization
-
G.M. Clore Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization Proc Natl Acad Sci USA 97 2000 9021 9025
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 9021-9025
-
-
Clore, G.M.1
-
38
-
-
0037433504
-
1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
-
1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics J Am Chem Soc 125 2003 2902 2912
-
(2003)
J Am Chem Soc
, vol.125
, pp. 2902-2912
-
-
Clore, G.M.1
Schwieters, C.D.2
-
39
-
-
3042807894
-
Model building of a protein-protein complexed structure using saturation transfer and residual dipolar coupling without paired intermolecular NOE
-
T. Matsuda, T. Ikegami, N. Nakajima, T. Yamazaki, and H. Nakamura Model building of a protein-protein complexed structure using saturation transfer and residual dipolar coupling without paired intermolecular NOE J Biomol NMR 29 2004 325 328 The authors describe the building of a complex model based on cross-saturation and residual dipolar coupling data. They take advantage of the higher sensitivity of cross-saturation compared to the NOESY experiment.
-
(2004)
J Biomol NMR
, vol.29
, pp. 325-328
-
-
Matsuda, T.1
Ikegami, T.2
Nakajima, N.3
Yamazaki, T.4
Nakamura, H.5
-
40
-
-
13844255387
-
Natively unfolded proteins
-
A.L. Fink Natively unfolded proteins Curr Opin Struct Biol 15 2005 35 41
-
(2005)
Curr Opin Struct Biol
, vol.15
, pp. 35-41
-
-
Fink, A.L.1
-
41
-
-
0036468397
-
Coupling of folding and binding for unstructured proteins
-
H.J. Dyson, and P.E. Wright Coupling of folding and binding for unstructured proteins Curr Opin Struct Biol 12 2002 54 60
-
(2002)
Curr Opin Struct Biol
, vol.12
, pp. 54-60
-
-
Dyson, H.J.1
Wright, P.E.2
-
42
-
-
0037203771
-
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
-
S.J. Demarest, M. Martinez-Yamout, J. Chung, H. Chen, W. Xu, H.J. Dyson, R.M. Evans, and P.E. Wright Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators Nature 415 2002 549 553
-
(2002)
Nature
, vol.415
, pp. 549-553
-
-
Demarest, S.J.1
Martinez-Yamout, M.2
Chung, J.3
Chen, H.4
Xu, W.5
Dyson, H.J.6
Evans, R.M.7
Wright, P.E.8
-
43
-
-
4344682825
-
The CBP/p300 TAZ1 domain in its native state is not a binding partner of MDM2
-
T. Matt, M.A. Martinez-Yamout, H.J. Dyson, and P.E. Wright The CBP/p300 TAZ1 domain in its native state is not a binding partner of MDM2 Biochem J 381 2004 685 691
-
(2004)
Biochem J
, vol.381
, pp. 685-691
-
-
Matt, T.1
Martinez-Yamout, M.A.2
Dyson, H.J.3
Wright, P.E.4
-
44
-
-
0037117479
-
Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha
-
S.J. Freedman, Z.Y. Sun, F. Poy, A.L. Kung, D.M. Livingston, G. Wagner, and M.J. Eck Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha Proc Natl Acad Sci USA 99 2002 5367 5372
-
(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 5367-5372
-
-
Freedman, S.J.1
Sun, Z.Y.2
Poy, F.3
Kung, A.L.4
Livingston, D.M.5
Wagner, G.6
Eck, M.J.7
-
45
-
-
0038392752
-
Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2
-
S.J. Freedman, Z.Y. Sun, A.L. Kung, D.S. France, G. Wagner, and M.J. Eck Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2 Nat Struct Biol 10 2003 504 512
-
(2003)
Nat Struct Biol
, vol.10
, pp. 504-512
-
-
Freedman, S.J.1
Sun, Z.Y.2
Kung, A.L.3
France, D.S.4
Wagner, G.5
Eck, M.J.6
-
46
-
-
12144255152
-
CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding
-
R.N. De Guzman, J.M. Wojciak, M.A. Martinez-Yamout, H.J. Dyson, and P.E. Wright CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding Biochemistry 44 2005 490 497
-
(2005)
Biochemistry
, vol.44
, pp. 490-497
-
-
De Guzman, R.N.1
Wojciak, J.M.2
Martinez-Yamout, M.A.3
Dyson, H.J.4
Wright, P.E.5
-
47
-
-
0033597729
-
The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1
-
P.E.C. Hershey, S.M. McWhirter, J.D. Gross, G. Wagner, T. Alber, and A.B. Sachs The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1 J Biol Chem 274 1999 21297 21304
-
(1999)
J Biol Chem
, vol.274
, pp. 21297-21304
-
-
Hershey, P.E.C.1
McWhirter, S.M.2
Gross, J.D.3
Wagner, G.4
Alber, T.5
Sachs, A.B.6
-
48
-
-
3543015540
-
Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation
-
J.R. Peterson, L.C. Bickford, D. Morgan, A.S. Kim, O. Ouerfelli, M.W. Kirschner, and M.K. Rosen Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation Nat Struct Mol Biol 11 2004 747 755 This paper describes the identification and characterization of wiskostatin, a chemical inhibitor of N-WASP. The NMR structure of the complex between wiskostatin and the regulatory GDP-binding domain (GBD) of N-WASP revealed that wiskostatin interacts with the cleft in the GBD and stabilizes its auto-inhibited structure.
-
(2004)
Nat Struct Mol Biol
, vol.11
, pp. 747-755
-
-
Peterson, J.R.1
Bickford, L.C.2
Morgan, D.3
Kim, A.S.4
Ouerfelli, O.5
Kirschner, M.W.6
Rosen, M.K.7
-
49
-
-
21744436606
-
Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region
-
M.A. Pufall, G.M. Lee, M.L. Nelson, H-S. Kang, A. Velyvis, L.E. Kay, L.P. McIntosh, and B.J. Graves Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region Science 309 2005 142 145 The authors revealed that phosphorylation of the unstructured region of the transcriptional activator Est-1 produces a graded DNA-binding affinity. NMR analysis of the Ets-1 structure indicates that phosphorylation of the unstructured region dynamically regulates the Ets-1 structure from a partially unfolded DNA-binding conformation to a well-folded inhibited conformation.
-
(2005)
Science
, vol.309
, pp. 142-145
-
-
Pufall, M.A.1
Lee, G.M.2
Nelson, M.L.3
Kang, H.-S.4
Velyvis, A.5
Kay, L.E.6
McIntosh, L.P.7
Graves, B.J.8
-
50
-
-
0029836953
-
Discovering high-affinity ligands for proteins: SAR by NMR
-
S.B. Shuker, P.J. Hajduk, R.P. Meadows, and S.W. Fesik Discovering high-affinity ligands for proteins: SAR by NMR Science 274 1996 1531 1534
-
(1996)
Science
, vol.274
, pp. 1531-1534
-
-
Shuker, S.B.1
Hajduk, P.J.2
Meadows, R.P.3
Fesik, S.W.4
-
51
-
-
20444486559
-
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
-
L based on the SAR by NMR approach is described. NMR-based screening followed by complex structure determination and structure-based optimization resulted in a low nanomolar inhibitor. To minimize uptake by HAS, the HAS spectrum was assigned and the compound was modified to prevent binding to HAS. The ABT-737 compound was shown to induce the regression of lymphoma and small-cell lung carcinoma in mice, and cure a high percentage of them.
-
(2005)
Nature
, vol.435
, pp. 677-681
-
-
Oltersdorf, T.1
Elmore, S.W.2
Shoemaker, A.R.3
Armstrong, R.C.4
Augeri, D.J.5
Belli, B.A.6
Bruncko, M.7
Deckwerth, T.L.8
Dinges, J.9
Hajduk, P.J.10
-
52
-
-
0033168872
-
High-throughput nuclear magnetic resonance-based screening
-
P.J. Hajduk, T. Gerfin, J.M. Boehlen, M. Haberli, D. Marek, and S.W. Fesik High-throughput nuclear magnetic resonance-based screening J Med Chem 42 1999 2315 2317
-
(1999)
J Med Chem
, vol.42
, pp. 2315-2317
-
-
Hajduk, P.J.1
Gerfin, T.2
Boehlen, J.M.3
Haberli, M.4
Marek, D.5
Fesik, S.W.6
-
53
-
-
4544371672
-
NMR-driven discovery of benzoylanthranilic acid inhibitors of far upstream element binding protein binding to the human oncogene c-myc promoter
-
J.R. Huth, L. Yu, I. Collins, J. Mack, R. Mendoza, B. Isaac, D.T. Braddock, S.W. Muchmore, K.M. Comess, and S.W. Fesik NMR-driven discovery of benzoylanthranilic acid inhibitors of far upstream element binding protein binding to the human oncogene c-myc promoter J Med Chem 47 2004 4851 4857 This paper describes the NMR-based discovery of an inhibitor of the far upstream element binding protein, which is essential for proto-oncogene c-myc expression. The authors tried both NMR-based and in silico screening. Interestingly, the NMR-derived hits were also in the library used for in silico screening, but were not ranked in the top 1000 compounds (from 584 000 compounds). However, the in silico screen contained two active molecules that were not in the library for NMR screens, which suggests the complementary use of these techniques.
-
(2004)
J Med Chem
, vol.47
, pp. 4851-4857
-
-
Huth, J.R.1
Yu, L.2
Collins, I.3
MacK, J.4
Mendoza, R.5
Isaac, B.6
Braddock, D.T.7
Muchmore, S.W.8
Comess, K.M.9
Fesik, S.W.10
-
54
-
-
0033213957
-
The SHAPES strategy: An NMR-based approach for lead generation in drug discovery
-
J. Fejzo, C.A. Lepre, J.W. Peng, G.W. Bemis, Ajay, M.A. Murcko, and J.M. Moore The SHAPES strategy: an NMR-based approach for lead generation in drug discovery Chem Biol 6 1999 755 769
-
(1999)
Chem Biol
, vol.6
, pp. 755-769
-
-
Fejzo, J.1
Lepre, C.A.2
Peng, J.W.3
Bemis, G.W.4
Ajay5
Murcko, M.A.6
Moore, J.M.7
-
55
-
-
16244380752
-
NMR techniques used with very large biological macromolecules in solution
-
G. Wider NMR techniques used with very large biological macromolecules in solution Methods Enzymol 394 2005 382 398
-
(2005)
Methods Enzymol
, vol.394
, pp. 382-398
-
-
Wider, G.1
-
58
-
-
0035692794
-
WaterLOGSY as a method for primary NMR screening: Practical aspects and range of applicability
-
C. Dalvit, G. Fogliatto, A. Stewart, M. Veronesi, and B. Stockman WaterLOGSY as a method for primary NMR screening: practical aspects and range of applicability J Biomol NMR 21 2001 349 359
-
(2001)
J Biomol NMR
, vol.21
, pp. 349-359
-
-
Dalvit, C.1
Fogliatto, G.2
Stewart, A.3
Veronesi, M.4
Stockman, B.5
-
59
-
-
0033789206
-
Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water
-
C. Dalvit, P. Pevarello, M. Tato, M. Veronesi, A. Vulpetti, and M. Sundstrom Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water J Biomol NMR 18 2000 65 68
-
(2000)
J Biomol NMR
, vol.18
, pp. 65-68
-
-
Dalvit, C.1
Pevarello, P.2
Tato, M.3
Veronesi, M.4
Vulpetti, A.5
Sundstrom, M.6
-
60
-
-
0034596286
-
Second-site NMR screening with a spin-labeled first ligand
-
W. Jahnke, L.B. Perez, C.G. Paris, A. Strauss, G. Fendrich, and C.M. Nalin Second-site NMR screening with a spin-labeled first ligand J Am Chem Soc 122 2000 7394 7395
-
(2000)
J Am Chem Soc
, vol.122
, pp. 7394-7395
-
-
Jahnke, W.1
Perez, L.B.2
Paris, C.G.3
Strauss, A.4
Fendrich, G.5
Nalin, C.M.6
-
61
-
-
24744449809
-
Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors
-
W. Jahnke, M.J. Blommers, C. Fernandez, C. Zwingelstein, and R. Amstutz Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors ChemBioChem 6 2005 1607 1610 Using the relaxation enhancement caused by a spin-labeled adenine analog, second-site inhibitors of the Bcr-Abl protein kinase were identified and used to optimize the primary inhibitor by fragment fusion.
-
(2005)
ChemBioChem
, vol.6
, pp. 1607-1610
-
-
Jahnke, W.1
Blommers, M.J.2
Fernandez, C.3
Zwingelstein, C.4
Amstutz, R.5
-
62
-
-
4143099131
-
Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer
-
T.K. Oost, C. Sun, R.C. Armstrong, A.S. Al-Assaad, S.F. Betz, T.L. Deckwerth, H. Ding, S.W. Elmore, R.P. Meadows, and E.T. Olejniczak Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer J Med Chem 47 2004 4417 4426 The authors developed a non-peptidic small-molecular inhibitor of XIAP based on the NMR structure of the SMAC peptide-XIAP complex. The non-peptidic compound possesses a stronger binding activity (5.6 μM) than the parent peptide (812 μM) while preserving the same binding mode. From this study, the authors claim that heterocycles such as thiazoles and imidazoles could serve as a replacement for the peptide fragment.
-
(2004)
J Med Chem
, vol.47
, pp. 4417-4426
-
-
Oost, T.K.1
Sun, C.2
Armstrong, R.C.3
Al-Assaad, A.S.4
Betz, S.F.5
Deckwerth, T.L.6
Ding, H.7
Elmore, S.W.8
Meadows, R.P.9
Olejniczak, E.T.10
-
63
-
-
25444487775
-
Monitoring the effects of antagonists on protein-protein interactions with NMR spectroscopy
-
L. D'Silva, P. Ozdowy, M. Krajewski, U. Rothweiler, M. Singh, and T.A. Holak Monitoring the effects of antagonists on protein-protein interactions with NMR spectroscopy J Am Chem Soc 127 2005 13220 13226
-
(2005)
J Am Chem Soc
, vol.127
, pp. 13220-13226
-
-
D'Silva, L.1
Ozdowy, P.2
Krajewski, M.3
Rothweiler, U.4
Singh, M.5
Holak, T.A.6
-
64
-
-
0035150803
-
Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL
-
A. Degterev, A. Lugovskoy, M. Cardone, B. Mulley, G. Wagner, T. Mitchison, and J. Yuan Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL Nat Cell Biol 3 2001 173 182
-
(2001)
Nat Cell Biol
, vol.3
, pp. 173-182
-
-
Degterev, A.1
Lugovskoy, A.2
Cardone, M.3
Mulley, B.4
Wagner, G.5
Mitchison, T.6
Yuan, J.7
-
65
-
-
2442714017
-
Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules
-
M.H. Roehrl, S. Kang, J. Aramburu, G. Wagner, A. Rao, and P.G. Hogan Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules Proc Natl Acad Sci USA 101 2004 7554 7559
-
(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 7554-7559
-
-
Roehrl, M.H.1
Kang, S.2
Aramburu, J.3
Wagner, G.4
Rao, A.5
Hogan, P.G.6
-
66
-
-
11144265736
-
A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization
-
M.H. Roehrl, J.Y. Wang, and G. Wagner A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization Biochemistry 43 2004 16056 16066
-
(2004)
Biochemistry
, vol.43
, pp. 16056-16066
-
-
Roehrl, M.H.1
Wang, J.Y.2
Wagner, G.3
-
67
-
-
11144347825
-
Discovery of small-molecule inhibitors of the NFAT-calcineurin interaction by competitive high-throughput fluorescence polarization screening
-
M.H. Roehrl, J.Y. Wang, and G. Wagner Discovery of small-molecule inhibitors of the NFAT-calcineurin interaction by competitive high-throughput fluorescence polarization screening Biochemistry 43 2004 16067 16075
-
(2004)
Biochemistry
, vol.43
, pp. 16067-16075
-
-
Roehrl, M.H.1
Wang, J.Y.2
Wagner, G.3
-
68
-
-
0037138678
-
A novel approach for characterizing protein ligand complexes: Molecular basis for specificity of small-molecule Bcl-2 inhibitors
-
A.A. Lugovskoy, A.I. Degterev, A.F. Fahmy, P. Zhou, J.D. Gross, J. Yuan, and G. Wagner A novel approach for characterizing protein ligand complexes: molecular basis for specificity of small-molecule Bcl-2 inhibitors J Am Chem Soc 124 2002 1234 1240
-
(2002)
J Am Chem Soc
, vol.124
, pp. 1234-1240
-
-
Lugovskoy, A.A.1
Degterev, A.I.2
Fahmy, A.F.3
Zhou, P.4
Gross, J.D.5
Yuan, J.6
Wagner, G.7
-
69
-
-
0037138706
-
TreeDock: A tool for protein docking based on minimizing van der Waals energies
-
A. Fahmy, and G. Wagner TreeDock: a tool for protein docking based on minimizing van der Waals energies J Am Chem Soc 124 2002 1241 1250
-
(2002)
J Am Chem Soc
, vol.124
, pp. 1241-1250
-
-
Fahmy, A.1
Wagner, G.2
-
70
-
-
31344452991
-
Folding transitions during assembly of the eukaryotic mRNA cap-binding complex
-
in press.
-
von der Haar T, Oku Y, Ptushkina M, Moerke N, Wagner G, Gross JD, McCarthy JEG: Folding transitions during assembly of the eukaryotic mRNA cap-binding complex. J Mol Biol 2006, in press.
-
(2006)
J Mol Biol
-
-
Von Der Haar, T.1
Oku, Y.2
Ptushkina, M.3
Moerke, N.4
Wagner, G.5
Gross, J.D.6
McCarthy, J.E.G.7
|