2000
1. Xiong Y; Juminaga D; Swapna GVT; Wedemayer WJ; Scheraga HA; Montelione GT. Protein Science. 2000, 9: 421 – 426. Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A. PMC2144552. Pubmed.
2. McDermott A; Polenova T; Bockmann A; Zilm KW; Paulson EK; Martin RW; Montelione GT. J. Biomol. NMR. 2000, 16: 209 – 219. Partial NMR resonance assignments of uniformly (13C,15N)-labeled BPTI in the solid state. Pubmed.
3. Montelione GT; Anderson S. The Investigational Drugs Database (IDdb). March 15, 2000. Quantitative challenges in the post-genomic sequence era.
4. Andrec M; Inman KG; Weber DJ; Levy RM; Montelione GT. J. Magn. Reson. 2000, 146: 66 – 80. A Bayesian statistical method for the detection and qualification of rotational diffusion anistropy from NMR relaxational data. Pubmed.
5. Andrec M; Montelione GT; Levy, R. J. Biomol. NMR. 2000, 18: 83 – 100. Lipari-Szabo mapping: A graphical approach to Lipari-Szabo analysis of NMR relaxation data using reduced spectral density mapping. Pubmed.
6. Montelione GT; Zheng D; Huang YJ; Gunsalus KC; Szyperski; T. Nature Struct. Biol. 2000, 7: 982 – 985. Protein NMR spectroscopy in structural genomics. Pubmed.
1999
1. Montelione GT; Anderson; S. Nature Struct. Biol. 1999, 6: 11 – 12. Structural genomics: Keystone for a human proteome project. Pubmed.
2. Wang W; Riedel K; Lynch P; Chien CY; Montelione GT; Krug RM. RNA. 1999, 5: 195 – 205. RNA-binding by the novel helical domain of the Influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids. PMC1369752. Pubmed.
3. Swapna GVT; Montelione GT. J. Magn. Reson. 1999, 137: 437 – 442. Sensitivity-enhanced Sim-CT HMQC PFG-HBHA(CO)NH and PFG-CBCA(CO)NH triple-resonance experiments. Pubmed.
4. Andrec M; Montelione GT; Levy RM. J. Magn. Reson. 1999, 139: 408 – 421. Estimation of dynamic parameters from NMR relaxation data using the Lipari-Szabo Model-free approach and Bayesian statistical methods. Pubmed.
5. Moseley HNB; Montelione, GT. Curr. Opin. Struct. Biol. 1999, 9: 635 – 642. Automated analysis of NMR assignments and structures for proteins. Pubmed.
6. Tejero R; Monleon D; Celda B; Montelione GT. J. Biomol. NMR. 1999, 15: 251 – 264. HYPER: A hierarchical algorithm for automatic determination of protein dihedral-angle constraints and stereospecific C βH2 resonance assignments from NMR data.
7. Laity JH; Montelione GT; Scheraga HA. Biochemistry. 1999, 38: 16432 – 16442. Comparison of local and global stability of an analogue of a disulfide-folding intermediate with those of the wild-type protein in bovine pancreatic ribonuclease A: Identification of specific regions of stable structure along the oxidative folding pathway. suppl. material. Pubmed.
8. Montelione GT; Rios CB; Swapna GVT; Zimmerman DE. 1999, Biological Magnetic Resonance, v 17: Structural Computation and Dynamics in Protein NMR, pp. 81 – 130. NMR pulse sequences and computational approaches for automated analysis of sequence- specific backbone resonance assignments in proteins. ‘
1998
1. Sahasrabudhe PV; Tejero R; Kitao S; Furuichi Y; Montelione GT. PROTEINS: Struct. Funct. Genetics. 1998, 33: 558 – 566. Homology modeling of an RNP domain from a human RNA-binding protein: Homology-constrained energy optimization provides a criterion for distinguishing potential sequence alignments. Pubmed.
2. Feng W; Tejero R; Zimmerman DE; Inouye M; Montelione GT. Biochemistry. 1998, 37: 10881 – 10896. Solution NMR structure and backbone dynamics of the major cold shock protein (CspA) from Escherichia coli Evidence for conformational dynamics in the ssRNA- binding site. suppl. material. Pubmed.
3. Montelione GT; Farid RS; Hitchcock-DeGregori SE. Biochemistry. 1998, 37: 7834 – 7843. The structure of the N-terminus of striated muscle α-tropomyosin in a chimeric peptide: Solution NMR structure and circular dichroism studies. suppl. material.
4. Mullenbach GT; Chiu CY; Gyenes A; Blaney J; Rosenberg S; Marlowe CK; Brown S; Stratton-Thomas J; Montelione GT; George- Nascimento C; Stauber G. Protein Engineering. 1998, 11: 473 – 480. Modification of a receptor-binding surface of epidermal growth factor (EGF): Analogs with enhanced receptor affinity at low pH or at neutrality. Pubmed.
5. Jin, D; Andrec M; Montelione GT; Levy RM. J. Biomol. NMR. 1998, 12: 471 – 492. Propagation of experimental uncertainties using the Lipari-Szabo model-free analysis of protein dynamics. Pubmed.
6. Kulikowski CA; Zimmerman D; Montelione GT; Anderson S. Stud. Health Technol. Inform. 1998, 52 Pt. 1: 365-366. Structural- functional bioinformatics: Knowledge-based NMR interpretation.
1997
1. Swapna GVT; Ríos CB; Shang Z; Montelione GT. J. Biomol. NMR. 1997, 9: 105 – 111. Application of multiple-quantum line narrowing with simultaneous 1H and 13C constant-time scalar- coupling evolution in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments. Pubmed.
2. Li H; Tejero R; Monleon D; Bassolino-Klimas D; Abate-Shen C; Bruccoleri RE; Montelione GT. Protein Science. 1997, 6: 956 – 970. Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: Application in predicting the three-dimensional structure of murine homeodomain Msx-1. PMC2143703. Pubmed.
3. Zimmerman DE; Kulikowski CA; Huang Y; Feng W; Tashiro M; Shimotakahara S; Chien CY; Powers R; Montelione GT. J. Mol. Biol. 1997, 269: 592 – 610. Automated analysis of protein NMR assignments using methods from artificial intelligence. Pubmed.
4. Shimotakahara S; Ríos CB; Laity JH; Zimmerman DE; Scheraga HA; Montelione GT. Biochemistry. 1997, 36 : 6915 – 6929. NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: Automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms. suppl. material. Pubmed.
5. Laity JH; Lester C; Shimotakahara S; Zimmerman DE; Montelione GT; Scheraga HA. Biochemistry. 1997, 36: 12683 – 12699. Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A. suppl. material. Pubmed.
6. Shang Z; Swapna GVT; Ríos CB; Montelione GT. J. Am. Chem. Soc. 1997, 119: 9274 – 9278. Sensitivity enhancement of triple-resonance protein NMR spectra by proton evolution of multiple-quantum coherences using a simultaneous 1H and 13C constant-time evolution period.
7. Tashiro M; Tejero R; Zimmerman DE; Celda B; Nilsson B; Montelione GT. J. Mol. Biol. 1997, 272: 573 – 590. High resolution solution NMR structure of the Z domain of staphylococcal protein A. Pubmed.
8. Chien CY; Tejero R; Huang Y; Zimmerman DE; Krug RM; Montelione GT. Nature Struct. Biol. 1997, 4: 891 – 895. A novel RNA-binding motif in influenza A virus non-structural protein 1. Pubmed.
9. Liu J; Lynch P; Chien CY; Montelione GT; Krug RM; Berman H. Nature Struct. Biol. 1997, 4: 896 – 899. Crystal structure of the unique RNA- binding domain of the influenza virus NS1 protein. Pubmed.
10. Jin D; Figueirido F; Montelione GT; Levy RM. J. Am. Chem. Soc. 1997, 119: 6923 – 6924. Impact of the precision in NMR relaxation measurements on the interpretation of protein dynamics.
1996
1. Jendeberg L; Tashiro M; Tejero R; Lyons BA; Uhlén M; Montelione GT; Nilsson B. Biochemistry 1996, 35: 22 – 31. The mechanism of binding staphylococcal protein A to immunoglobulin G does not involve helix unwinding. Pubmed.
2. Jansson M; Li YC; Jendeberg L; Anderson S; Montelione GT; Nilsson B. J. Biomol. NMR. 1996, 7: 131 – 141. High- level production of uniformly 15N-and 13C-enriched fusion proteins in Escherichia coli. Pubmed.
3. Bassolino-Klimas D; Tejero R; Krystek SR; Metzler WJ; Montelione GT; Bruccoleri RE. Protein Science. 1996, 5: 593 – 603. Simulated annealing with restrained molecular dynamics using a flexible restraint potential: Theory and evaluation with simulated NMR constraints. PMC2143380. Pubmed.
4. Tejero R; Bassolino-Klimas D; Bruccoleri RE; Montelione GT. Protein Science. 1996, 5: 578 – 592. Simulated annealing with restrained molecular dynamics using CONGEN: Energy refinement of the NMR solution structures of epidermal and type-α transforming growth factors. PMC2143379.
5. Feng W; Ríos CB; Montelione G. T. J. Biomol. NMR. 1996, 8: 98 – 104. Phase labeling of C-H and C-C spin-system topologies: Applications in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments for determining backbone resonance assignments in proteins. Pubmed.
6. Ríos CB; Feng W; Tashiro M; Shang Z; Montelione GT. J. Biomol. NMR. 1996, 8: 345 – 350. Phase labeling of C-H and C-C spin system topologies: Application in constant-time PFG-CBCA(CO)NH experiments for discriminating amino-acid spin-system types. Pubmed.
1995
1. Tashiro M; Montelione GT. Current Opin. In Struct. Biol. 1995, 5: 471 – 481. Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins. Pubmed.
2. Zimmerman DE; Montelione GT. Current Opin. in Struct. Biol. 1995, 5: 664 – 673. Automated analysis of nuclear magnetic resonance assignments for proteins. Pubmed.
3. Celda B; Biamonti C; Arnau MJ; Tejero R; Montelione GT. J. Biomol. NMR. 1995, 5: 161 – 172. Combined use of 13C chemical shift and 1Hα–13Cα heteronuclear NOE data in monitoring a protein NMR structure refinement. Pubmed.
4. Li YC; Montelione GT. Biochemistry. 1995, 34: 2408 – 2423. Human type- α transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by 15N relaxation measurements. Pubmed.
5. Tashiro M; Ríos CB, Montelione GT. J. Biomol. NMR. 1995, 6: 211 – 216. Classification of amino acid spin systems using PFG HCC(CO)NH-TOCSY with constant-time aliphatic carbon-13 frequency labeling. Pubmed.
6. Fadel AR; Jin DQ; Montelione GT; Levy RM. J. Biomol. NMR. 1995, 6: 221 – 226. Crankshaft motions of the polypeptide backbone in molecular dynamics simulations of human type-α transforming growth factor. Pubmed.
7. Qian XY; Chien CY; Lu Y; Montelione GT; Krug RM. RNA. 1995, 1: 948 – 956. An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure. PMC1369343.
1994
1. Campion SR; Biamonti C; Montelione GT; Niyogi SK. Protein Engineering. 1993, 6: 651 – 659. The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. (featured on cover of August 1994 issue of Protein Engineering).
2. Lyons BA; Tashiro M; Cedergren L, Nilsson B; Montelione GT. Biochemistry. 1993, 32: 7839 – 7845. An improved strategy for determining resonance assignments for isotopically enriched proteins and its application on an engineered domain of staphylococcal Protein A.
3. Li YC; Montelione GT. J. Magn. Reson. 1993, B101: 315 – 319. Solvent saturation-transfer effects in pulsed-field-gradient heteronuclear single- quantum coherence (PFG-HSQC) spectra of polypeptides and proteins.
4. Zimmerman D; Kulikowski C; Montelione GT. Proc. Int. Conf. Intell. Syst. Mol. Biol. 1993, 1: 447 – 455. A constraint reasoning system for automating sequence-specific resonance assignments in multidimensional protein NMR spectra.
5. Zimmerman D; Kulikowski C; Wang L; Lyons B; Montelione GT. J. Biomol. NMR. 1994, 4: 241 – 256. Automated sequencing of amino acid spin systems in proteins using multidimensional HCC(CO)NH-TOCSY spectroscopy and constraint propagation methods from artificial intelligence.
6. Li YC; Montelione GT. J. Magn. Reson. 1994, 105: 45 – 51. Overcoming solvent saturation-transfer artifacts in protein NMR at neutral pH: Application of pulsed-field gradients in measurements of1H- 15N Overhauser effects.
7. Newkirk K; Feng W; Jiang W; Tejero R; Emerson SD; Inouye M; Montelione GT. Proc. Natl. Acad. Sci. U.S.A. 1994, 91: 5114 – 5118. Solution NMR structure of the major cold-shock protein (CspA) from Escherichia coli : Identification of a binding epitope for DNA. PMC43942.
8. Shang Z; Isaac VE; Li H; Patel L; Catron KM; Curran T; Montelione GT; Abate C. Proc. Natl. Acad. Sci. U.S.A. 1994, 91: 8373 – 8377. Design of a “minimA1” homeodomain: the N- terminal arm modulates DNA binding affinity and stabilizes homeodomain structure. PMC44608.
9. Biamonti C; Ríos CB; Lyons BA; Montelione GT. Advances in Biophysical Chemistry. 1994, 4: 51 – 120. Multidimensional NMR experiments and analysis techniques for determining homo- and heteronuclear scalar coupling constants in proteins and nucleic acids.
1993
1. Lyons BA; Montelione GT. J. Magn. Reson. 1993, B101: 206 – 209. An HCCNH triple-resonance experiment using carbon-13 isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins.
2. Celda B; Montelione GT. J. Magn. Reson. 1993, B101: 189 – 193. Total correlation spectroscopy (TOCSY) of proteins using coaddition of spectra recorded with several mixing times.
3. Moy FJ; Li YC; Rauenbuehler P; Winkler ME; Scheraga HA; Montelione GT. Biochemistry. 1993, 32: 7334 – 7353. Solution structure of human type-α transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints. suppl. material.
4. Campion SR; Biamonti C; Montelione GT; Niyogi SK. Protein Engineering. 1993, 6: 651 – 659. The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. (featured on cover of August 1994 issue of Protein Engineering).
5. Lyons BA; Tashiro M; Cedergren L; Nilsson B; Montelione GT. Biochemistry. 1993, 32: 7839 – 7845. An improved strategy for determining resonance assignments for isotopically enriched proteins and its application on an engineered domain of staphylococcal Protein A.
6. Li YC; Montelione GT. J. Magn. Reson. 1993, B101: 315 – 319. Solvent saturation-transfer effects in pulsed-field-gradient heteronuclear single- quantum coherence (PFG-HSQC) spectra of polypeptides and proteins.
7. Zimmerman D; Kulikowski C; Montelione GT. Proc. Int. Conf. Intell. Syst. Mol. Biol. 1993, 1: 447 – 455. A constraint reasoning system for automating sequence-specific resonance assignments in multidimensional protein NMR spectra.
1992
1. Montelione GT; Wüthrich K; Burgess AW; Nice EC; Wagner G; Gibson KD; Scheraga HA. Biochemistry. 1992, 31: 236 – 249. Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints.
2. Emerson SD; Montelione GT. J. Amer. Chem. Soc. 1992, 114: 354 – 356. Accurate measurements of proton scalar coupling constants using carbon-13 isotropic mixing spectroscopy.
3. Montelione GT; Emerson SD; Lyons BA. Biopolymers. 1992, 32: 327 – 334. A general approach for determining scalar coupling constants in polypeptides and proteins.
4. Moy FJ; Scheraga HA; Patt SL; Montelione GT. J. Magn. Reson. 1992, 98: 451 – 457. Application of frequency-shifted shaped pulses for overcoming solvent-saturation transfer and pre-irradiation associated spin-diffusion effects in aqueous solutions of polypeptides and proteins.
5. Emerson SD; Montelione GT. J. Magn. Reson. 1992, 99: 413 – 420. 2D and 3D HCCH TOCSY experiments for determining 3J(Hα-Hβ) coupling constants of amino acid residues.
6. Montelione GT; Lyons BA; Emerson SD; Tashiro M. J. Amer. Chem. Soc. 1992, 114: 10974 – 10975. An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically enriched proteins. suppl. material.
1990
1. Wagner G; Nirmala NR; Montelione GT; Hyberts S. Frontiers of NMR in Molecular Biology. 129 – 143. 1990. A.R. Liss, Inc., New York, NY. Static and dynamic aspects of protein structure.
2. Montelione, G.T.; Wagner, G. J. Magn. Reson. 1990, 87: 183 – 188. Conformation-independent sequential NMR connections in isotope-enriched polypeptides by 1H-13C- 15N triple-resonance experiments.
3. Engler, D.A.; Montelione, G.T.; Niyogi, S.K. FEBS Lett. 1990, 271: 47 – 50. Human epidermal growth factor: Distinct roles of Tyr-37 and Arg-41 in receptor binding as determined by site-directed mutagenesis and nuclear magnetic resonance spectroscopy.
1989
1. Montelione, G.T.; Winkler, M.E.; Burton, L.E.;Rinderknecht, E.; Sporn, M.B.; Wagner, G. Proc. Natl. Acad. Sci. U.S.A. 1989, 86: 1519 – 1523. Sequence-specific 1H-NMR assignments and identification of two small anti-parallel β-sheets in the solution structure of recombinant human transforming growth factor-α. PMC286729
2. Montelione, G.T.; Wagner, G. J. Amer. Chem. Soc. 1989, 111: 3096 – 3098. 2D chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation.
3. Montelione, G.T.; Winkler, M.; Rauenbuehler, P.; Wagner,G. J. Magn. Reson. 1989, 82: 198 – 204. Accurate measurements of long-range heteronuclear coupling constants from homonuclear 2D NMR spectra of isotope- enriched proteins.
4. Montelione, G.T.; Wagner, G. J. Amer. Chem. Soc. 1989, 111: 5474 – 5475. Accurate measurements of homonuclear HN-Hα coupling constants in polypeptides using heteronuclear 2D NMR experiments. (pdf)
5. Moy, F.J.; Scheraga, H.A.; Liu, J.-F.; Wu, R.; Montelione, G.T. Proc. Natl. Acad. Sci. U.S.A. 1989, 86: 9836 – 9840. Conformational characterization of a single-site mutant of murine epidermal growth factor (EGF) by 1H-NMR provides evidence that leucine-47 is involved in interactions with the EGF receptor. PMC298597
6. Montelione, G.T.; Scheraga, H.A. Accts. Chem. Research 1989, 22: 70 – 76. Formation of local structures in protein folding.
1988
1. Montelione, G.T.; Wüthrich, K.; Scheraga, H.A. Biochemistry 1988, 27: 2235 – 2243. Sequence-specific 1H-NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth factor. suppl. material
2. Ray, P.; Moy, F.; Montelione, G.T.; Liu, J.-F.; Narang, S.A.; Scheraga, H.A.; Wu, R. Biochemistry 1988, 27: 7289 – 7295. Structure- function studies of murine epidermal growth factor: Expression and site- directed mutagenesis of the epidermal growth factor gene.
1987
1. Talluri S; Montelione GT; Van Duyne G; Piela L; Clardy J; Scheraga HA. J. Amer. Chem. Soc. 1987, 109: 4473 – 4477. Conformational properties of 2,4-methanoproline (2,carboxy-2,4-methanopyrrolidine) in peptides: Evidence for 2,4-methanopyrrolidine asymmetry based on solid state X-ray crystallography, 1H-NMR in aqueous solution, and CNDO/2 conformational energy calculations. suppl. material.
2. Haas E; Montelione GT; McWherter CA; Scheraga HA. Biochemistry. 1987, 26: 1672 – 1682. Local structure in a tryptic fragment of performic acid oxidized ribonuclease A corresponding to a proposed polypeptide chain-folding initiation site detected by tyrosine fluorescence lifetime and proton magnetic resonance measurements.
3. Montelione GT; Wüthrich K; Nice EC; Burgess AW; Scheraga HA. Proc. Natl. Acad. Sci. U.S.A. 1987, 84: 5226 – 5230. Solution structure of murine epidermal growth factor: Determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry. PMC298827.
1986
1. Stimson ER; Meinwald YC; Montelione GT; Scheraga HA. Intl. J. Peptide Protein Res. 1986, 27: 569 – 582. Conformational properties of trans Ac- Asn-Pro-Tyr-NHMe and trans Ac-Tyr-Pro-Asn-NHMe in dimethylsulfoxide and in water determined by multinuclear NMR spectroscopy.
2. Montelione GT; Hughes P; Clardy J; Scheraga HA. J. Amer. Chem. Soc. 1986, 108: 6765 – 6773. Conformational properties of 2,4-methanoproline (2-carboxy-2,4-methanopyrrolidine) in peptides: Determination of preferred peptide bond conformations in aqueous solution by proton Overhauser measurements.
3. Montelione GT; Wüthrich K; Nice EC; Burgess AW; Scheraga HA. Proc. Natl. Acad. Sci. U.S.A. 1986, 83: 8594 – 8598. Identification of two anti-parallel beta-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance. PMC386977.
1984
1. Montelione GT; Arnold E; Meinwald YC; Stimson ER; Denton JB; Huang SG; Clardy J; Scheraga HA. J. Amer. Chem. Soc. 1984, 106: 7946 – 7958. Chain-folding initiation structures in ribonuclease A: Conformational analysis of trans Ac-Asn-Pro-Tyr-NHMe and trans Ac-Tyr-Pro-Asn-NHMe in water and in the solid state. suppl. material addition/correction.
2. Oka M; Montelione GT; Scheraga HA. J. Amer. Chem. Soc. 1984, 106: 7959 – 7969. Chain-folding initiation structures in ribonuclease A: Conformational free energy calculations on Ac-Asn-Pro-Tyr- NHMe, Ac-Tyr-Pro-Asn-NHMe, and related peptides. suppl. material.
3. Swadesh JK; Montelione GT; Thannhauser TW; Scheraga HA. Proc. Natl. Acad. Sci. U.S.A. 1984, 81: 4606 – 4610. Local structure involving histidine-12 in reduced S-sulfonated ribonuclease A detected by proton NMR spectroscopy under folding conditions. PMC345642.
1982
1. Stimson ER; Montelione GT; Meinwald YC; Rudolph RKE; Scheraga HA. Biochemistry. 1982, 21: 5252 – 5262. Equilibrium ratios of cis– and trans-proline conformers in fragments of ribonuclease A from nuclear magnetic resonance spectra of adjacent tyrosine ring resonances. suppl. material.
1981
1. Montelione, G.T.; Callahan, S.; Podleski, T.R. Biochim. Biophys. Acta 1981 , 670: 110 – 123. Physical and chemical characterization of the major lactose-blockable lectin activity from fetal calf skeletal muscle.