H. K. Schachman

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Howard K Schachman, H.k. Schachman, H. K. Schachman, Howard K. Schachman, H K Schachman
Publication record
225 papers · 9,773 citations · H-index 50

PAPERS

Ultracentifugation in biochemistry
20161 citationsauthor #1
Synthesis of aspartate transcarbam Transcriptional regulation of the pnh
20160 citationsauthor #2
ACID: AN INTERRUPTED TWO-STRAND MODEL*
20160 citationsauthor #2
Perspectives and Conclusions
201518 citationsauthor #2
Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase.
200943 citationsauthor #2
Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase.
200931 citationsauthor #2
A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase
200792 citationsauthor #3
From “Publish or Perish” to “Patent and Prosper”
200635 citationsauthor #1
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation
20063 citationsauthor #3
Those wonderful early years with the Model E ultracentrifuge and David Yphantis.
20041 citationsauthor #1
On scientific freedom and responsibility.
20020 citationsauthor #1
Differential Scanning Calorimetry of Aspartate Transcarbamoylase and Its Isolated Subunits *
20020 citationsauthor #3
STRUCTURE OF THE R105A MUTANT CATALYTIC TRIMER OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE AT 2.0-A RESOLUTION
20020 citationsauthor #4
Quantitative urea gradient gel electrophoresis for studies of dissociation and unfolding of oligomeric proteins.
20023 citationsauthor #2
In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains
20019 citationsauthor #2
Random circular permutation leading to chain disruption within and near α helices in the catalytic chains of aspartate transcarbamoylase: Effects on assembly, stability, and function
200119 citationsauthor #6
22 Impact of Regulations on the Conduct of Research
20011 citationsauthor #1
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation induced cell migration.
200023 citationsauthor #4
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.
200028 citationsauthor #4
Still looking for the Ivory Tower.
20009 citationsauthor #1
Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit.
199930 citationsauthor #4
In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: Implications for protein folding and assembly
199656 citationsauthor #2
Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase.
199692 citationsauthor #2
Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Implications for domain switching
19969 citationsauthor #2
A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains.
19965 citationsauthor #2
Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Characterization of the active site and evidence for an interdomain carboxy‐terminal helix in ornithine transcarbamoylase
199618 citationsauthor #2
A 70‐amino acid zinc‐binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer
19943 citationsauthor #4
Association of the catalytic subunit of aspartate transcarbamoylase with a zinc‐containing polypeptide fragment of the regulatory chain leads to increases in thermal stability
19945 citationsauthor #5
What is misconduct in science?
199356 citationsauthor #1
Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains.
199338 citationsauthor #2
Remembering Bill Harrington
19931 citationsauthor #3
In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains
199311 citationsauthor #2
Asparate transcarbamoylase: Current opinion in structural biology 1993, 3:960–967
19935 citationsauthor #1
Peptide‐protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase
199310 citationsauthor #2
Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains
19939 citationsauthor #4
13C and 15N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase.
199214 citationsauthor #4
Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase.
199213 citationsauthor #3
Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits.
199210 citationsauthor #7
Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase.
199213 citationsauthor #3
Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.
199217 citationsauthor #2
13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase.
199219 citationsauthor #3
Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine.
199216 citationsauthor #6
The contribution of threonine 55 to catalysis in aspartate transcarbamoylase.
19928 citationsauthor #7
1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.
19922 citationsauthor #3
13C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate.
199211 citationsauthor #3
A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity.
199111 citationsauthor #3
Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase.
199114 citationsauthor #2
Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.
199113 citationsauthor #2
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.
199043 citationsauthor #3
Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects.
199026 citationsauthor #2
Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP.
198934 citationsauthor #3
Analytical ultracentrifugation reborn
198939 citationsauthor #1
Boundary spreading in sedimentation velocity experiments on partially liganded aspartate transcarbamoylase. A ligand-mediated isomerization.
198910 citationsauthor #3
Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments.
198926 citationsauthor #2
Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.
198928 citationsauthor #3
Attenuation in the regulation of the pyrBI operon in Escherichia coli. In vivo studies of transcriptional termination.
198912 citationsauthor #3
Preliminary Results on the Crystal and Molecular Structure of Native and Mutant Aspartate Carbamoyltransferase at Neutral pH
19883 citationsauthor #3
Formation of Active Aspartate Transcarbamoylase from Defective Polypeptide Chains Produced by Site-Directed Mutagenesis
19881 citationsauthor #3
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase.
198825 citationsauthor #3
Can a simple model account for the allosteric transition of aspartate transcarbamoylase?
198887 citationsauthor #1
From allostery to mutagenesis: 20 years with aspartate transcarbamoylase.
198712 citationsauthor #1
Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis.
198783 citationsauthor #2
Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase.
198713 citationsauthor #2
Kinetics of the interaction of N-(phosphonacetyl)-L-aspartate with the catalytic subunit of aspartate transcarbamoylase. A slow conformational change subsequent to binding.
198613 citationsauthor #2
Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.
198629 citationsauthor #6
Communication between polypeptide chains in aspartate transcarbamoylase. Conformational changes at the active sites of unliganded chains resulting from ligand binding to other chains.
19869 citationsauthor #2
19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits.
198514 citationsauthor #2
On conformational changes in the regulatory enzyme aspartate transcarbamoylase.
19854 citationsauthor #3
Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase.
198559 citationsauthor #2
Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?
198545 citationsauthor #2
19F nuclear magnetic resonance studies of communication between catalytic and regulatory subunits in aspartate transcarbamoylase.
19856 citationsauthor #2
Regulation of aspartate transcarbamoylase synthesis in Escherichia coli: analysis of deletion mutations in the promoter region of the pyrBI operon.
198521 citationsauthor #2
Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity.
198423 citationsauthor #2
Mercurial-promoted Zn2+ release from Escherichia coli aspartate transcarbamoylase.
198480 citationsauthor #3
The influence of quaternary structure on the active site of an oligomeric enzyme. Catalytic subunit of aspartate transcarbamoylase.
19847 citationsauthor #2
Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coli.
19842 citationsauthor #5
Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation.
198454 citationsauthor #1
Assembly of aspartate transcarbamoylase in Escherichia coli.
19832 citationsauthor #1
Assembly of Aspartate Transcarbamoylase in Escherichia colia
19834 citationsauthor #1
Synthesis of aspartate transcarbamoylase in Escherichia coli: transcriptional regulation of the pyrB-pyrI operon.
198337 citationsauthor #2
Communication between catalytic and regulatory subunits in Ni(II)- and Co(II)-aspartate transcarbamoylase. Ligand-promoted structural alterations at the intersubunit bonding domains.
198321 citationsauthor #2
Genetic characterization of the folding domains of the catalytic chains in aspartate transcarbamoylase.
198312 citationsauthor #2
Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains.
198229 citationsauthor #2
Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon.
198228 citationsauthor #4
Ligand-promoted strengthening of interchain bonding domains in catalytic subunits of aspartate transcarbamoylase.
19827 citationsauthor #2
Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers.
198235 citationsauthor #2
Linkage between reactivity of sulfhydryl groups and subunit interactions in aspartate transcarbamoylase.
19827 citationsauthor #2
On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase.
198115 citationsauthor #3
Spectral alterations associated with the ligand-promoted gross conformational change in aspartate transcarbamoylase.
19817 citationsauthor #3
The mechanism of dissociation of aspartate transcarbamoylase by p-mercuribenzoate.
198111 citationsauthor #2
Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli.
198113 citationsauthor #3
Communication between subunits in aspartate transcarbamoylase. Effect of active site ligands on the tertiary structure of regulatory chains.
19818 citationsauthor #4
Crystallization and preliminary X-ray diffraction studies of an inactive mutant aspartate transcarbamoylase from Escherichia coli.
19815 citationsauthor #3
Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: effect of active-site ligands on the regulatory chains.
198016 citationsauthor #2
Mechanism of disproportionation of asparate transcarbamoylase molecules lacking one regulatory subunit.
19804 citationsauthor #2
Equilibrium and kinetic studies of the association of catalytic and regulatory subunits of aspartate transcarbamoylase.
198015 citationsauthor #2
The ultracentrifuge: A retrospective and prospective view
19800 citationsauthor #1
Assembly of catalytic subunits of aspartate transcarbamoylase from Escherichia coli.
19802 citationsauthor #2
pryB mutations as suppressors of arginine auxotrophy in Salmonella typhimurium
19807 citationsauthor #2
A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits.
198010 citationsauthor #2

TIMELINE

1940 12 citations

1942 3 citations

1947 10 citations

1948 8 citations

1949 138 citations

1950 20 citations

1951 41 citations

1952 361 citations

1953 37 citations

1954 182 citations

1955 214 citations

1956 399 citations

1957 770 citations

1958 163 citations

1959 1,334 citations

1960 356 citations

1962 307 citations

1963 228 citations

1964 0 citations

1965 392 citations

1966 420 citations

1967 269 citations

1968 558 citations

1969 120 citations

1970 122 citations

1971 339 citations

1972 166 citations

1973 167 citations

1974 79 citations

1975 22 citations

1976 73 citations

1977 248 citations

1978 180 citations

1979 84 citations

1980 70 citations

1981 59 citations

1982 106 citations

1983 76 citations

1984 166 citations

1985 149 citations

1986 51 citations

1987 108 citations

1988 116 citations

1989 149 citations

1990 69 citations

1991 38 citations

1992 123 citations

1993 130 citations

1994 8 citations

1996 180 citations

1999 30 citations

2000 60 citations

2001 29 citations

2002 3 citations

2004 1 citations

2006 38 citations

2007 92 citations

2009 74 citations

2015 18 citations

2016 1 citations

H. K. Schachman

PROFILE

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