About: Carl Frieden

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American biophysicist

Attributes	Values
rdf:type	Item
field of work	wds:Q120681716-0a9116c9-461c-624e-9581-0a07174264c6
field of work	biophysics
description	American biophysicist (en) investigador d'Estaos Xuníos (ast)
rdfs:label	Carl Frieden (en) Carl Frieden (ast)
skos:prefLabel	Carl Frieden (en) Carl Frieden (ast)
name	Carl Frieden (en) Carl Frieden (ast)
National Academy of Sciences member ID	wds:Q120681716-a73ad753-487a-a04b-664b-dee177ceef6a
National Academy of Sciences member ID	8940
instance of	wds:Q120681716-C0B4F4BE-741D-4484-9852-720AC96D42A8
instance of	Homo sapiens
award received	wds:Q120681716-c6014450-4a7d-52fb-0ddc-3232327f4085
award received	Fellow of the American Academy of Arts and Sciences
doctoral advisor	wds:Q120681716-dd734819-45d6-69b8-e3b4-486992ca452f
doctoral student	wds:Q120681716-3443230a-43e2-82fd-ce1d-24dc1853218a wds:Q120681716-896e6fc0-44f4-1455-934b-2aee3ec066f8
Academic Tree ID	wds:Q120681716-22e64c3c-4fc8-89c6-f97f-3fb60abac6fb
doctoral advisor	Robert A. Alberty
doctoral student	Roberta F. Colman Paul E. Bock
Academic Tree ID	81387
ResearchGate profile ID	wds:Q120681716-74397CCB-F235-465E-A88C-ACA76629F158
ResearchGate profile ID	Carl-Frieden
occupation	wds:Q120681716-8D593898-F681-4377-8117-19291EA3B9FE
employer	wds:Q120681716-f53523c7-43e7-373c-ca35-96cf58b4741e
languages spoken, written or signed	wds:Q120681716-e8c588de-4e8f-5722-6e60-9bdf1cec78ef
place of birth	wds:Q120681716-1229b3db-4a15-0de6-b885-acb18757f79e
sex or gender	wds:Q120681716-cdf1a2ae-4aea-f7ba-a638-c7f1f7a3db0c
VIAF ID	wds:Q120681716-A516C35D-A90A-4795-811C-EE37465BB76D
country of citizenship	wds:Q120681716-fd26173b-4d57-985b-e47b-19faa8084662
educated at	wds:Q120681716-6a4e83ee-4b07-d8f9-8bde-5a8f3cc3fcd7 wds:Q120681716-80165c29-4704-e208-448e-71b99f432698
National Library of Israel J9U ID	wds:Q120681716-9B342F61-08F1-48B0-B95D-67C5C5F115E5
official website	wds:Q120681716-6ea30c32-444b-0f10-497b-c803e6e585b6
VIAF ID	http://viaf.org/viaf/94342672
occupation	researcher
employer	Washington University School of Medicine
languages spoken, written or signed	English
place of birth	New Rochelle
sex or gender	male
VIAF ID	94342672
country of citizenship	United States of America
educated at	University of Wisconsin–Madison Carleton College
National Library of Israel J9U ID	987007377185905171
official website	https://biochem.wustl.edu/cflab/
ORCID iD	wds:Q120681716-51DD243A-98B2-4239-8FD6-3918E154EE97
ORCID iD	https://orcid.org/0000-0002-4471-2427
ORCID iD	0000-0002-4471-2427
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q120681716
is pr:P3452 of	wdref:027c42d2681b1c991473fa8316fe82473d86aaa3
is author of	Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions TREATMENT OF ENZYME KINETIC DATA. I. THE EFFECT OF MODIFIERS ON THE KINETIC PARAMETERS OF SINGLE SUBSTRATE ENZYMERS Microheterogeneity of actin gels formed under controlled linear shear Polymerization and gelation of actin studied by fluorescence photobleaching recovery Actin polymerization. The mechanism of action of cytochalasin D Self-association and stability of the ApoE isoforms at low pH: implications for ApoE-lipid interactions Analysis of progress curves by simulations generated by numerical integration Climate change and the integrity of science Microinjection of gelsolin into living cells Slow Transitions and Hysteretic Behavior in Enzymes Catalysis of protein folding by chaperones in pathogenic bacteria A fluorescent probe for conformational changes in skeletal muscle G-actin Differences in G-actin containing bound ATP or ADP: the Mg2+-induced conformational change requires ATP ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions Concerning the structure of apoE Dissociation of apolipoprotein E oligomers to monomer is required for high-affinity binding to phospholipid vesicles NMR and protein folding: equilibrium and stopped-flow studies The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR. Expression and purification of amyloid-beta peptides from Escherichia coli Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase. Kinetic studies on the effect of yeast cofilin on yeast actin polymerization Protein aggregation processes: In search of the mechanism The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods PapD-like chaperones provide the missing information for folding of pilin proteins The Role of Zn 2+ on the Structure and Stability of Murine Adenosine Deaminase † What fluorescence correlation spectroscopy can tell us about unfolded proteins Intestinal fatty acid binding protein: characterization of mutant proteins containing inserted cysteine residues Intestinal fatty acid binding protein: folding of fluorescein-modified proteins Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases Actin and tubulin polymerization: the use of kinetic methods to determine mechanism Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL. Protein-protein interaction and enzymatic activity Glutamate dehydrogenase concentration as a determinant in the effect of purine nucleotides on enzymatic activity Identification of the sites of modification of bovine liver glutamate dehydrogenase reacted with trinitrobenzenesulfonate Effect of temperature on the mechanism of actin polymerization. pH-induced changes in G-actin conformation and metal affinity The Mg2+-induced conformational change in rabbit skeletal muscle G-actin ApoE: the role of conserved residues in defining function Polymerization of actin and actin-like systems: evaluation of the time course of polymerization in relation to the mechanism.

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