science
plus
.abes.fr
|
explorer
À propos de :
Ackers Gary K.
Goto
Sponge
NotDistinct
Permalink
An Entity of Type :
foaf:Person
, within Data Space :
scienceplus.abes.fr
associated with source
document(s)
Type:
Person
New Facet based on Instances of this Class
Attributs
Valeurs
type
Person
name
Ackers Gary K.
familyName
Ackers
Given name
Gary K.
is
relates
of
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_31/101021bi00245a023/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1976/volume_15/issue_3/101021bi00648a032/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1964/volume_3/issue_5/101021bi00893a021/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1976/volume_15/issue_24/101021bi00669a024/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1984/volume_23/issue_4/101021bi00299a004/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_19/101021bi00019a009/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1975/volume_14/issue_23/101021bi00694a017/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1979/volume_18/issue_15/101021bi00582a025/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1982/volume_21/issue_2/101021bi00531a001/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1986/volume_25/issue_23/101021bi00371a016/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_29/101021bi00243a031/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/1981/volume_20/issue_26/101021bi00529a018/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1984/volume_23/issue_10/101021bi00305a020/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_34/101021bi00200a015/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1982/volume_21/issue_5/101021bi00534a010/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_1/101021bi00116a010/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_10/101021bi00010a001/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1984/volume_23/issue_6/101021bi00301a029/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_27/101021bi00027a005/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_38/101021bi0493923/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_38/101021bi049393v/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_36/101021bi050710n/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_36/101021bi050709o/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_37/101021bi000935s/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1993/volume_32/issue_35/101021bi00086a012/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1990/volume_29/issue_42/101021bi00494a003/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1969/volume_8/issue_9/101021bi00837a049/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1990/volume_29/issue_28/101021bi00480a004/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1985/volume_24/issue_12/101021bi00333a037/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_36/101021bi00151a033/authorship/7
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_28/101021bi00194a003/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_49/101021bi00253a005/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_29/101021bi00243a030/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_31/101021bi00245a022/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_45/101021bi00160a032/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_28/101021bi00194a004/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1976/volume_15/issue_24/101021bi00669a023/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1974/volume_13/issue_11/101021bi00708a022/authorship/2
is
Author
of
Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates
Energetics of cooperative protein-DNA interactions: comparison between quantitative deoxyribonuclease footprint titration and filter binding
Linkage between cooperative oxygenation and subunit assembly of cobaltous human hemoglobin
Isolation of .lambda. repressor mutants with defects in cooperative operator binding
Molecular Exclusion and Restricted Diffusion Processes in Molecular-Sieve Chromatography*
Calorimetric determination of the heat of oxygenation of human hemoglobin as a function of pH and the extent of reaction
Enthalpic and Entropic Components of Cooperativity for the Partially Ligated Intermediates of Hemoglobin Support a "Symmetry Rule" Mechanism
Long-Range, Small Magnitude Nonadditivity of Mutational Effects in Proteins
Calorimetric Analysis of .lambda. cI Repressor Binding to DNA Operator Sites
Molecular sieve studies of interacting protein systems. V. Association of subunits of D-amino acid oxidase apoenzyme
Effects of inositol hexasulfate on the oxygen affinity of hemoglobin: verification of the integral function theory of thermodynamic linkage
Experimental resolution of cooperative free energies for the ten ligation species of cobalt(II)/iron(II)-carbon monoxide hemoglobin
Cooperative protein-DNA interactions: effects of potassium chloride on .lambda. cI binding to OR
Linkage between oxygenation and subunit dissociation in human hemoglobin. Consequences for the analysis of oxygenation curves
Proton-linked contributions to site-specific interactions of .lambda. cI repressor and OR
Energetics of subunit dimerization in bacteriophage .lambda. cI repressor: linkage to protons, temperature, and KCl
Self-Assembly of Bacteriophage .lambda. cI Repressor: Effects of Single-Site Mutations on the Monomer-Dimer Equilibrium
Bohr Effects of the Partially-Ligated (CN-met) Intermediates of Hemoglobin as Probed by Quaternary Assembly
Self-association and DNA binding of .lambda. cI repressor N-terminal domains reveal linkage between sequence-specific binding and the C-terminal cooperativity domain
Asymmetric Distribution of Cooperativity in the Binding Cascade of NormalHuman Hemoglobin. 2. Stepwise Cooperative Free Energy
The Molecular Code for Hemoglobin Allostery Revealed by Linking theThermodynamics and Kinetics of Quaternary Structural Change. 2. CooperativeFree Energies of (αFeCOβFe)2 and (αFeβFeCO)2 T-State Tetramers
Asymmetric Distribution of Cooperativity in the Binding Cascade of NormalHuman Hemoglobin. 1. Cooperative and Noncooperative Oxygen Binding inZn-Substituted Hemoglobin
Coupled Energetics of λ cro Repressor Self-Assembly and Site-Specific DNAOperator Binding I: Analysis of cro Dimerization from Nanomolar to MicromolarConcentrations
The Molecular Code for Hemoglobin Allostery Revealed by Linking theThermodynamics and Kinetics of Quaternary Structural Change. 1.Microstate Linear Free Energy Relations
Linked functions in allosteric proteins: an exact theory for the effect of organic phosphates on oxygen affinity of hemoglobin
Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin
Effects of protons on the oxygenation-linked subunit assembly in human hemoglobin
Site-specific enthalpic regulation of DNA transcription at bacteriophage .lambda. OR
Thermodynamic analysis of human hemoglobins in terms of the Perutz mechanism: extensions of the Szabo Karplus model to include subunit assembly
Effects of ionic strength and state of assembly on kinetics of hydrogen exchange of calf thymus histones
Measurement of DNA-protein equilibria using gel chromatography: application to the HinfI restriction endonuclease
Direct and indirect pathways of functional coupling in human hemoglobin are revealed by quantitative low-temperature isoelectric focusing of mutant hybrids
Single-Site Mutations in the C-Terminal Domain of Bacteriophage .lambda. cI Repressor Alter Cooperative Interactions between Dimers Adjacently Bound to OR
Oxygenation-linked subunit interactions in human hemoglobin: analysis of linkage functions for constituent energy terms
Electrostatic contributions to the energetics of dimer-tetramer assembly in human hemoglobin: pH dependence and effect of specifically bound chloride ions
Interactions of the nucleosomal core histones: a calorimetric study of octamer assembly
Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves
Functional properties of human hemoglobins synthesized from recombinant mutant .beta.-globins
Alternative Linked Data Documents:
ODE
Content Formats:
RDF
ODATA
Microdata
