Carl Frieden American biophysicist
Frieden, Carl, 1928-
![Sudoc [ABES], France](/viaf/images/flags/SUDOC.png "Sudoc [ABES], France")
Frieden, C.
Frieden, Carl
VIAF ID: 94342672 (Personal)
Permalink: http://viaf.org/viaf/94342672
Preferred Forms
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100 0 _
‡a
Carl Frieden
‡c
American biophysicist
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100 1 _ ‡a Frieden, C.
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100 1 _ ‡a Frieden, Carl
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100 1 _ ‡a Frieden, Carl ‡d (1928- ).
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100 1 _
‡a
Frieden, Carl
‡d
1928-
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100 1 _
‡a
Frieden, Carl,
‡d
1928-
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100 1 _ ‡a Frieden, Carl, ‡d 1928-
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100 1 _
‡a
Frieden, Carl,
‡d
1928-
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100 1 0
‡a
Frieden, Carl,
‡d
1928-
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100 1 _ ‡a Frieden, Carl, ‡d 1928-
4xx's: Alternate Name Forms (4)
Works
| Title | Sources |
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| Kinetic studies of the enzyme fumarase. |
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| Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4. |
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| Mechanism for nucleotide exchange in monomeric actin |
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| The mechanism of ligand-induced structural changes in glutamate dehydrogenase. Studies of the rate of depolymerization and isomerization effected by coenzymes and guanine nucleotides. |
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| Microheterogeneity of actin gels formed under controlled linear shear |
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| Microinjection of gelsolin into living cells |
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| Model dehydrogenase reaction. Charge distribution in the transition state |
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| The molecular weight of chicken-liver glutamate dehydrogenase |
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| Myoadenylate deaminase deficiency |
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| Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures |
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| Native Mass Spectrometry, Ion Mobility, Electron-Capture Dissociation, and Modeling Provide Structural Information for Gas-Phase Apolipoprotein E Oligomers |
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| New PC versions of the kinetic-simulation and fitting programs, KINSIM and FITSIM. |
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| NMR and protein folding: equilibrium and stopped-flow studies |
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| Numerical integration of rate equations by computer: an update. |
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| Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR. |
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| On the kinetic distinction of ordered and random bireactant enzyme systems |
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| PapD-like chaperones provide the missing information for folding of pilin proteins |
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| Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli |
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| pH-induced changes in G-actin conformation and metal affinity |
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| pH-induced cold lability of rabbit skeletal muscle phosphofructokinase. |
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| Polymerization-induced changes in the fluorescence of actin labeled with iodoacetamidotetramethylrhodamine |
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| Possible locally driven folding pathways of TC5b, a 20-residue protein |
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| The preparation of 19F-labeled proteins for NMR studies |
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| Preparation, purification and properties of a crosslinked trimer of G-actin |
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| Protein aggregation processes: In search of the mechanism |
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| Protein folding: how the mechanism of GroEL action is defined by kinetics |
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| Protein fragments as probes in the study of protein folding mechanisms: differential effects of dihydrofolate reductase fragments on the refolding of the intact protein |
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| Protein oligomerization as a metabolic control mechanism: Application to apoE |
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| Protein-protein interactions |
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| Protein structural changes accompanying formation of enzymatic transition states: tryptophan environment in ground-state and transition-state analogue complexes of adenosine deaminase. |
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| The purification and physical properties of glutamate dehydrogenase from rat liver |
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| Purification of GroEL with low fluorescence background |
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| Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ |
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| Rabbit muscle phosphofructokinase. Modification of molecular and regulatory kinetic properties with the affinity label 5'-p-(fluorosulfonyl)benzoyl adenosine |
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| Rabbit muscle phosphofructokinase: studies of the subunit molecular weight and structure. Isolation of carboxymethylated cysteinyl peptides and sedimentation equilibrium studies |
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| Rabbit muscle phosphofructokinase: studies on the polymerization. The behavior of the enzyme at pH 8, pH 6, and intermediate pH values |
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| The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: implications for the mechanism. |
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| Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. |
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| The regulation of protein polymerization |
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| RELATIONSHIP BETWEEN SUBUNIT STRUCTURE AND ACTIVITY FOR BEEF LIVER GLUTAMIC DEHYDROGENASE |
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| The Role of Zn 2+ on the Structure and Stability of Murine Adenosine Deaminase † |
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| The search for local native-like nucleation centers in the unfolded state of beta -sheet proteins |
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| Self-association and stability of the ApoE isoforms at low pH: implications for ApoE-lipid interactions |
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| Slow Transitions and Hysteretic Behavior in Enzymes |
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| A small computer system for the routine analysis of enzyme kinetic mechanisms |
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| Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation |
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| Steady-state and time-resolved fluorescence studies of the intestinal fatty acid binding protein. |
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| Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase |
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| Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease |
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| Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR. |
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| Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation |
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| The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism |
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| Studies on the structure of actin gels using time correlation spectroscopy of fluorescent beads |
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| Substoichiometric inhibition of Abeta(1-40) aggregation by a tandem Abeta(40-1-Gly8-1-40) peptide |
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| Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase |
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| Treatment of enzyme kinetic data. 3. The use of the full time course of a reaction, as examined by computer simulation, in defining enzyme mechanisms |
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| TREATMENT OF ENZYME KINETIC DATA. I. THE EFFECT OF MODIFIERS ON THE KINETIC PARAMETERS OF SINGLE SUBSTRATE ENZYMERS |
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| Treatment of enzyme kinetic data. II. The multisite case: comparison of allosteric models and a possible new mechanism. |
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| Turn scanning by site-directed mutagenesis: application to the protein folding problem using the intestinal fatty acid binding protein |
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| Turn scanning. Experimental and theoretical approaches to the role of turns |
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| The tyrosine B10 hydroxyl is crucial for oxygen avidity of Ascaris hemoglobin |
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| Understanding Curli Amyloid-Protein Aggregation by Hydrogen-Deuterium Exchange and Mass Spectrometry |
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| Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation |
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| The unusual inhibition of glutamate dehydrogenase by guanosine di- and triphosphate |
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| Urea-dependent unfolding of murine adenosine deaminase: sequential destabilization as measured by 19F NMR. |
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| The use of the fluorescence photobleaching recovery technique to study the self-assembly of tubulin |
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| The Washington University Medical Scientist Training Program. |
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| What fluorescence correlation spectroscopy can tell us about unfolded proteins |
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| Yeast actin: polymerization kinetic studies of wild type and a poorly polymerizing mutant |
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