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Thermodynamic Properties of the Redox Centers of Na+-Translocating NADH:Quinone Oxidoreductase
Thermodynamic Properties of the Redox Centers of Na+-Translocating NADH:Quinone Oxidoreductase
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Thermodynamic Properties of the Redox Centers of Na+-Translocating NADH:Quinone Oxidoreductase

Bogachev, Alexander V ; Bertsova, Yulia V ; Bloch, Dmitry A ; Verkhovsky, Michael I

Biochemistry (Easton), 2006-03, Vol.45 (10), p.3421-3428 [Periódico revisado por pares]

United States: American Chemical Society

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2
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
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Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid

Estefania P. C. Azevedo Humberto D'Muniz Pereira; Richard Charles Garratt; Jeffery W Kelly; Debora Foguel; Fernando L Palhano

Biochemistry Washington, DC : American Chemical Society - ACS v. 50, n. 51, p. 11070-11083, Dec. 2011

Washington, DC 2011

Localização: IFSC - Inst. Física de São Carlos    (PROD019201 )(Acessar)

3
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
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Artigo 		Adicionar ao Meu Espaço

Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid

Estefania P. C. Azevedo Humberto D'Muniz Pereira; Richard Charles Garratt; Jeffery W Kelly; Debora Foguel; Fernando L Palhano

Biochemistry Washington, DC : American Chemical Society - ACS v. 50, n. 51, p. 11070-11083, Dec. 2011

Washington, DC 2011

Localização: IFSC - Inst. Física de São Carlos    (PROD019201 )(Acessar)

4
Effect of Basic Cell-Penetrating Peptides on the Structural, Thermodynamic, and Hydrodynamic Properties of a Novel Drug Delivery Vector, ELP[V5G3A2‑150]
Effect of Basic Cell-Penetrating Peptides on the Structural, Thermodynamic, and Hydrodynamic Properties of a Novel Drug Delivery Vector, ELP[V5G3A2‑150]
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Effect of Basic Cell-Penetrating Peptides on the Structural, Thermodynamic, and Hydrodynamic Properties of a Novel Drug Delivery Vector, ELP[V5G3A2‑150]

Lyons, Daniel F ; Le, Vu ; Kramer, Wolfgang H ; Bidwell, Gene L ; Lewis, Edwin A ; Raucher, Drazen ; Correia, John J

Biochemistry (Easton), 2014-02, Vol.53 (6), p.1081-1091 [Periódico revisado por pares]

United States: American Chemical Society

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5
“Designing Out” Disulfide Bonds:  Thermodynamic Properties of 30−51 Cystine Substitution Mutants of Bovine Pancreatic Trypsin Inhibitor
“Designing Out” Disulfide Bonds:  Thermodynamic Properties of 30−51 Cystine Substitution Mutants of Bovine Pancreatic Trypsin Inhibitor
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“Designing Out” Disulfide Bonds:  Thermodynamic Properties of 30−51 Cystine Substitution Mutants of Bovine Pancreatic Trypsin Inhibitor

Liu, Yi ; Breslauer, Kenneth ; Anderson, Stephen

Biochemistry (Easton), 1997-05, Vol.36 (18), p.5323-5335 [Periódico revisado por pares]

United States: American Chemical Society

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6
Characterization of the Photophysical, Thermodynamic, and Structural Properties of the Terbium(III)–DREAM Complex
Characterization of the Photophysical, Thermodynamic, and Structural Properties of the Terbium(III)–DREAM Complex
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Characterization of the Photophysical, Thermodynamic, and Structural Properties of the Terbium(III)–DREAM Complex

Gonzalez, Walter G ; Ramos, Victoria ; Diaz, Maurizio ; Garabedian, Alyssa ; Molano-Arevalo, Juan Camilo ; Fernandez-Lima, Francisco ; Miksovska, Jaroslava

Biochemistry (Easton), 2016-03, Vol.55 (12), p.1873-1886 [Periódico revisado por pares]

United States: American Chemical Society

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7
Accuracy and Precision of a New H/D Exchange- and Mass Spectrometry-Based Technique for Measuring the Thermodynamic Properties of Protein−Peptide Complexes
Accuracy and Precision of a New H/D Exchange- and Mass Spectrometry-Based Technique for Measuring the Thermodynamic Properties of Protein−Peptide Complexes
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Accuracy and Precision of a New H/D Exchange- and Mass Spectrometry-Based Technique for Measuring the Thermodynamic Properties of Protein−Peptide Complexes

Powell, Kendall D ; Fitzgerald, Michael C

Biochemistry (Easton), 2003-05, Vol.42 (17), p.4962-4970 [Periódico revisado por pares]

United States: American Chemical Society

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8
Lung surfactant proteins, SP-B and SP-C, alter the thermodynamic properties of phospholipid membranes: a differential calorimetry study
Lung surfactant proteins, SP-B and SP-C, alter the thermodynamic properties of phospholipid membranes: a differential calorimetry study
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Lung surfactant proteins, SP-B and SP-C, alter the thermodynamic properties of phospholipid membranes: a differential calorimetry study

Shiffer, Kathleen ; Hawgood, Samuel ; Haagsman, Henk P ; Benson, Bradley ; Clements, John A ; Goerke, Jon

Biochemistry (Easton), 1993-01, Vol.32 (2), p.590-597 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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9
Thermodynamic Properties of the Transition State for the Rate-Limiting Step in the Folding of the .alpha. Subunit of Tryptophan Synthase
Thermodynamic Properties of the Transition State for the Rate-Limiting Step in the Folding of the .alpha. Subunit of Tryptophan Synthase
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Thermodynamic Properties of the Transition State for the Rate-Limiting Step in the Folding of the .alpha. Subunit of Tryptophan Synthase

Chen, Xiaowu ; Matthews, C. Robert

Biochemistry (Easton), 1994-05, Vol.33 (20), p.6356-6362 [Periódico revisado por pares]

United States: American Chemical Society

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10
Expression, Folding, and Thermodynamic Properties of the Bovine Oxytocin−Neurophysin Precursor:  Relationships to the Intermolecular Oxytocin−Neurophysin Complex
Expression, Folding, and Thermodynamic Properties of the Bovine Oxytocin−Neurophysin Precursor:  Relationships to the Intermolecular Oxytocin−Neurophysin Complex
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Expression, Folding, and Thermodynamic Properties of the Bovine Oxytocin−Neurophysin Precursor:  Relationships to the Intermolecular Oxytocin−Neurophysin Complex

Eubanks, Sharon ; Lu, Min ; Peyton, David ; Breslow, Esther

Biochemistry (Easton), 1999-10, Vol.38 (41), p.13530-13541 [Periódico revisado por pares]

United States: American Chemical Society

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Deste Autor:

  1. Foguel, D
  2. Azevedo, E
  3. Garratt, R
  4. Pereira, H
  5. Kelly, J

Neste Assunto:

  1. Science & Technology
  2. Life Sciences & Biomedicine
  3. Biochemistry & Molecular Biology
  4. Thermodynamics
  5. Kinetics

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