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Accurate Protein Crystallography at Ultra-High Resolution: Valence Electron Distribution in Crambin

Proceedings of the National Academy of Sciences - PNAS, 2000-03, Vol.97 (7), p.3171-3176

2000

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Myoglobin cavities provide interior ligand pathway

Protein science, 2004-02, Vol.13 (2), p.313-318

Teeter, Martha M.

2004

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Crystal Structure of C-Phycocyanin from Cyanidium caldarium Provides a New Perspective on Phycobilisome Assembly

Biophysical journal, 1999-06, Vol.76 (6), p.2912-2921

1999

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An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D2 and D3 Receptors

Molecular pharmacology, 2009-01, Vol.75 (1), p.19

2009

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Modeling and Mutational Analysis of a Putative Sodium-Binding Pocket on the Dopamine D2 Receptor

Molecular pharmacology, 2001-08, Vol.60 (2), p.373-381

2001

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Identification of a Zn2+-binding site on the dopamine D2 receptor

Biochemical and biophysical research communications, 2006-01, Vol.339 (3), p.873-879

2006

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CoMFA-Based Prediction of Agonist Affinities at Recombinant Wild Type versus Serine to Alanine Point Mutated D2 Dopamine Receptors

Journal of medicinal chemistry, 2000-08, Vol.43 (16), p.3005-3019

2000

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Harmonic and quasiharmonic descriptions of crambin

Journal of physical chemistry (1952), 1990-10, Vol.94 (21), p.8091-8097

1990

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Homology Modeling of the Dopamine D2 Receptor and Its Testing by Docking of Agonists and Tricyclic Antagonists

Journal of medicinal chemistry, 1994-09, Vol.37 (18), p.2874-2888

1994

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Atomic Resolution (0·83 Å) Crystal Structure of the Hydrophobic Protein Crambin at 130 K

Journal of molecular biology, 1993-03, Vol.230 (1), p.292-311

1993

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Experimental Observation of Bonding Electrons in Proteins

The Journal of biological chemistry, 1999-07, Vol.274 (30), p.20753-20755

1999

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An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D 2 and D 3 Receptors

Molecular pharmacology, 2009-01, Vol.75 (1), p.19-26

2009

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Crystal Structure of Ser-22/Ile-25 Form Crambin Confirms Solvent, Side Chain Substate Correlations

The Journal of biological chemistry, 1997-04, Vol.272 (15), p.9597-9600

1997

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Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur

Nature (London), 1981-03, Vol.290 (5802), p.107-113

1981

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Primary structure of the hydrophobic plant protein crambin

Biochemistry (Easton), 1981-09, Vol.20 (19), p.5437-5443

1981

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An empirical examination of potential-energy minimization using the well-determined structure of the protein crambin

Journal of the American Chemical Society, 1986-11, Vol.108 (23), p.7163-7172

1986

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Structural Determinants of Pharmacological Specificity Between D 1 and D 2 Dopamine Receptors

Molecular pharmacology, 2006-01, Vol.69 (1), p.185-194

2006

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Identification of binding determinants for arrestin on D2 dopamine receptor intracellular loops

The FASEB journal, 2009-04, Vol.23 (S1)

2009

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Raman spectroscopy of homologous plant toxins: crambin and .alpha.1- and .beta.-purothionin secondary structures, disulfide conformation, and tyrosine environment

Biochemistry (Easton), 1984-12, Vol.23 (26), p.6796-6802

1984

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An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D2 and D3 Receptors1

Molecular pharmacology, 2009-01, Vol.75 (1), p.19-26

2009

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Assemblies of Alzheimer’s peptides Aβ25–35 and Aβ31–35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction

Journal of structural biology, 2003-02, Vol.141 (2), p.156-170

2003

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Assemblies of Alzheimer's peptides A beta 25-35 and A beta 31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction

Journal of structural biology, 2003-02, Vol.141 (2), p.156

2003

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Crystal structure of α‐hordothionin at 1.9 Å resolution

FEBS letters, 2005-04, Vol.579 (11), p.2301-2306

2005

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Modeling and Mutational Analysis of a Putative Sodium-Binding Pocket on the Dopamine D 2 Receptor

Molecular pharmacology, 2001-08, Vol.60 (2), p.373-381

2001

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Water-protein interactions : theory and experiment

Annual review of biophysics and biophysical chemistry, 1991-06, Vol.20 (1), p.577-600

TEETER, M. M

1991

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Accurate Protein Crystallography at Ultra-High Resolution: Valence Electron Distribution in Crambin

Myoglobin cavities provide interior ligand pathway

Crystal Structure of C-Phycocyanin from Cyanidium caldarium Provides a New Perspective on Phycobilisome Assembly

An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D2 and D3 Receptors

Modeling and Mutational Analysis of a Putative Sodium-Binding Pocket on the Dopamine D2 Receptor

Identification of a Zn2+-binding site on the dopamine D2 receptor

CoMFA-Based Prediction of Agonist Affinities at Recombinant Wild Type versus Serine to Alanine Point Mutated D2 Dopamine Receptors

Harmonic and quasiharmonic descriptions of crambin

Homology Modeling of the Dopamine D2 Receptor and Its Testing by Docking of Agonists and Tricyclic Antagonists

Atomic Resolution (0·83 Å) Crystal Structure of the Hydrophobic Protein Crambin at 130 K

Experimental Observation of Bonding Electrons in Proteins

An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D 2 and D 3 Receptors

Crystal Structure of Ser-22/Ile-25 Form Crambin Confirms Solvent, Side Chain Substate Correlations

Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur

Primary structure of the hydrophobic plant protein crambin

An empirical examination of potential-energy minimization using the well-determined structure of the protein crambin

Structural Determinants of Pharmacological Specificity Between D 1 and D 2 Dopamine Receptors

Identification of binding determinants for arrestin on D2 dopamine receptor intracellular loops

Raman spectroscopy of homologous plant toxins: crambin and .alpha.1- and .beta.-purothionin secondary structures, disulfide conformation, and tyrosine environment

An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D2 and D3 Receptors1

Assemblies of Alzheimer’s peptides Aβ25–35 and Aβ31–35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction

Assemblies of Alzheimer's peptides A beta 25-35 and A beta 31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction

Crystal structure of α‐hordothionin at 1.9 Å resolution

Modeling and Mutational Analysis of a Putative Sodium-Binding Pocket on the Dopamine D 2 Receptor

Water-protein interactions : theory and experiment

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