Howard Kapnek Schachman

Howard Kapnek Schachman's AcademicInfluence.com Rankings

Biology

#3941

World Rank

#5952

Historical Rank

#1546

USA Rank

Biochemistry

#404

World Rank

#482

Historical Rank

#154

USA Rank

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Biology

Howard Kapnek Schachman's Degrees

PhD Biochemistry University of California, Berkeley
Bachelors Chemistry University of California, Berkeley

Why Is Howard Kapnek Schachman Influential?

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According to Wikipedia, Howard Kapnek Schachman was a graduate school professor in the Department of Molecular & Cell Biology at the University of California, Berkeley. Early life Schachman was born in Philadelphia in 1918. In high school, he was interested in sociopolitical issues, inspired by his mother. He initially pursued liberal arts in college while studying to become a rabbi, before switching to chemical engineering in a university. He transferred from the University of Pennsylvania to the Massachusetts Institute of Technology, where he graduated in 1939 with a chemical engineering degree.

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Howard Kapnek Schachman's Published Works

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Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author

Published Works

Ultracentrifugation in biochemistry (1959) (994)
[2] Ultracentrifugation, diffusion, and viscometry (1957) (569)
Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase. (1965) (391)
The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. (1967) (270)
Ultracentrifuge Studies with Rayleigh Interference Optics.I. General Application (1959) (248)
Enzymatic synthesis of deoxyribonucleic acid. VII. Synthesis of a polymer of deoxyadenylate and deoxythymidylate. (1960) (240)
Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. (1968) (237)
Studies on the macro-molecular organization of microbial cells. (1952) (234)
Ultracentrifuge studies with absorption optics. IV. Molecular weight determinations at the microgram level. (1966) (213)
The isolation and characterization of a macromolecular ribonucleoprotein from yeast (1956) (179)
Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits. (1968) (167)
Ultracentrifuge studies with Rayleigh interference optics. II. Low-speed sedimentation equilibrium of homogeneous systems. (1968) (154)
The dissociation and reconstitution of aldolase. (1962) (151)
Ultracentrifugal analysis of dilute solutions. (1957) (144)
Studies on the validity of the Einstein viscosity law and Stokes' law of sedimentation (1955) (125)
Complexes of silver ion with natural and synthetic polynucleotides (1966) (124)
ULTRACENTRIFUGE STUDIES WITH RAYLEIGH INTERFERENCE OPTICS. III. COMPUTATIONAL METHODS APPLIED TO HIGH‐SPEED SEDIMENTATION EQUILIBRIUM EXPERIMENTS * (1969) (116)
The hydration, size and shape of tobacco mosaic virus. (1949) (112)
Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model. (1977) (98)
A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase (2007) (92)
Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase. (1996) (91)
Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. (1977) (91)
THE ULTRACENTRIFUGE: PROBLEMS AND PROSPECTS. (1963) (87)
Can a simple model account for the allosteric transition of aspartate transcarbamoylase? (1988) (87)
Ultracentrifuge studies with absorption optics. II. Incorporation of a monochromator and its application to the study of proteins and interacting systems. (1962) (83)
Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. (1987) (81)
Ultracentrifugation Studies with Absorption Optics. V. Analysis of Interacting Systems Involving Macromolecules and Small Molecules (1966) (80)
Mercurial-promoted Zn2+ release from Escherichia coli aspartate transcarbamoylase. (1984) (80)
Molecular-weight determinations during the approach to sedimentation equilibrium. (1956) (79)
On the molecular weight of myosin. (1958) (78)
Structure and arrangement of the regulatory subunits in aspartate transcarbamylase. (1972) (77)
ULTRACENTRIFUGE STUDIES WITH ABSORPTION OPTICS. 3. A SPLIT-BEAM PHOTOELECTRIC, SCANNING ABSORPTION SYSTEM. (1963) (75)
Ultracentrifuge studies with absorption optics. I. An automatic photoelectric scanning absorption system. (1962) (74)
On the size of the protein subunits in bushy stunt virus. (1958) (74)
A role for zinc in the quaternary structure of aspartate transcarbamylase from Escherichia coli. (1972) (71)
Studies on the organization of nucleic acids within nucleoproteins (1960) (71)
A Study of the Kinetics of the Enzymatic Digestion of Deoxyribonucleic Acid1 (1956) (70)
Considerations on the Tertiary Structure of Proteins (1963) (66)
Studies on the alkaline degradation of tobacco mosaic virus. I. Ultracentrifugal analysis. (1956) (66)
Chromatophores of Rhodospirillum rubrum (1952) (62)
Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase. (1971) (60)
In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: Implications for protein folding and assembly (1996) (60)
Hybridization of native and chemically modified enzymes. I. Development of a general method and its application to the study of the subunit structure of aldolase. (1970) (60)
Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase. (1985) (59)
A sedimentation equilibrium method for determining molecular weights of proteins with a tabletop high speed air turbine centrifuge. (1978) (58)
Studies on the Contractile Proteins of Muscle. I. The ATP-Myosin B Interaction1,2 (1959) (57)
Conformational changes in proteins as measured by difference sedimentation studies. I. A technique for measuring small changes in sedimentation coefficient. (1971) (56)
Sedimentation equilibrium studies on glutamic dehydrogenase. (1971) (55)
Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation. (1984) (54)
What is misconduct in science? (1993) (53)
Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. I. Focusing of the camera and cylindrical lenses. (1971) (50)
The Determination of Concentrations in the Ultracentrifugation of Two‐Component Systems (1954) (50)
Characterization of cyanobacterial phycobilisomes in zwitterionic detergents. (1979) (48)
Protein-ligand binding studies with a table-top, air-driven high-speed centrifuge. (1978) (47)
Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate? (1985) (46)
Dissociation of hemoglobin into subunits. Monomer formation and the influence of ligands. (1971) (46)
[4] Measurement of partial specific volume by sedimentation equilibrium in H2OD2O solutions (1973) (46)
Studies on the sedimentation behaviour of thymus deoxypentose nucleic acid with reference to its homogeneity, size and shape. (1954) (45)
Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase. (2009) (45)
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase. (1990) (43)
Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. II. A general procedure. (1971) (41)
Analytical ultracentrifugation reborn (1989) (38)
Analysis of a Concentration Anomaly in the Ultracentrifugation of Mixtures1 (1953) (38)
[5] Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits (1978) (37)
Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains. (1993) (37)
An Ultracentrifuge Cell for Producing Boundaries Synthetically by a Layering Technique. (1952) (36)
Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites. (1976) (36)
Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers. (1982) (35)
A DIFFERENTIAL ULTRACENTRIFUGE TECHNIQUE FOR MEASURING SMALL CHANGES IN SEDIMENTATION COEFFICIENTS1 (1957) (35)
The sedimentation of deoxyribonucleic acid in three component systems. (1955) (35)
Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP. (1989) (34)
From “Publish or Perish” to “Patent and Prosper” (2006) (34)
Synthesis of aspartate transcarbamoylase in Escherichia coli: transcriptional regulation of the pyrB-pyrI operon. (1983) (34)
ON THE MACROMOLECULAR STRUCTURE OF DEOXYRIBONUCLEIC ACID: AN INTERRUPTED TWO-STRAND MODEL. (1954) (34)
Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits. (1977) (33)
Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase. (1970) (32)
Ultracentrifugal studies with absorption optics and a split-beam photoelectric scanner. (1973) (31)
Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit. (1999) (30)
Hybridization of native and chemically modified enzymes. II. Native and succinylated glyceraldehyde 3-phosphate dehydrogenase. (1970) (30)
Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase. (2009) (30)
Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase. (1986) (29)
Effect of D2O and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenase. (1973) (29)
Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains. (1982) (29)
Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon. (1982) (28)
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation. (2000) (27)
Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects. (1990) (27)
Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains. (1989) (27)
Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments. (1989) (26)
Studies on the enzymatic breakdown of proteins. I. Action of chymotrypsin on insulin. (1960) (25)
Local and gross conformational changes in aspartate transcarbamylase. (1973) (25)
Differential scanning calorimetry of asparate transcarbamoylase and its isolate subunits. (1978) (24)
Ultracentrifuge Studies with a Synthetic Boundary Cell.1II. Differential Sedimentation (1955) (24)
Ultracentrifuge Studies on Tobacco Mosaic Virus (1951) (24)
Viscosity and sedimentation studies on tobacco mosaic virus. (1949) (24)
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase. (1988) (24)
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation induced cell migration. (2000) (23)
Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity. (1984) (23)
Communication between catalytic and regulatory subunits in Ni(II)- and Co(II)-aspartate transcarbamoylase. Ligand-promoted structural alterations at the intersubunit bonding domains. (1983) (22)
Anatomy and physiology of a regulatory enzyme-aspartate transcarbamylase. (1974) (21)
Alteration of the allosteric properties of aspartate transcarbamoylase by pyridoxylation of the catalytic and regulatory subunits. (1976) (21)
The Density Correction of Sedimentation Constants (1950) (20)
Regulation of aspartate transcarbamoylase synthesis in Escherichia coli: analysis of deletion mutations in the promoter region of the pyrBI operon. (1985) (19)
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 (2001) (19)
13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase. (1992) (19)
Perspectives and Conclusions (2015) (18)
ON VISCOSITY MEASUREMENT IN THE ULTRACENTRIFUGE1 (1952) (18)
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 (1996) (18)
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. (1992) (17)
A disproportionation mechanism for the all-or-none dissociation of mercurial-treated glyceraldehyde phosphate dehydrogenase. (1971) (17)
Conformational studies on the nitrated catalytic subunit of aspartate transcarbamylase. (1973) (17)
Cooperative interactions in aspartate transcarbamoylase. 1. Hybrids composed of native and chemically inactivated catalytic polypeptide chains. (1974) (17)
On the state of the parental phosphorus during reproduction of bacteriophage T2. (1954) (17)
A method for the separation of hybrids of chromatographically identical oligomeric proteins. Use of 3,4,5,6-tetrahydrophthaloyl groups as a reversible "chromatographic handle". (1976) (17)
Physical Chemical Studies on Rabbit Papilloma Virus1 (1951) (16)
Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: effect of active-site ligands on the regulatory chains. (1980) (16)
Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine. (1992) (16)
Aspartate transcarbamoylase molecules lacking one regulatory subunit. (1974) (16)
ULTRACENTRIFUGE, ELECTROPHORESIS, AND VISCOSITY STUDIES ON CRYSTALLINE PYROPHOSPHATASE (1952) (16)
Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains. (1980) (16)
Equilibrium and kinetic studies of the association of catalytic and regulatory subunits of aspartate transcarbamoylase. (1980) (15)
Studies on the enzymatic breakdown of proteins. II. The action of pepsin on ribonuclease and considerations of the structure of ribonuclease. (1960) (15)
Physical studies on the ribonucleic acid of turnip yellow mosaic virus. (1957) (15)
On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase. (1981) (15)
13C and 15N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase. (1992) (14)
Reactivation of enzymes by light-stimulated cleavage of reduced pyridoxal 5'-phosphate-enzyme complexes. (1977) (14)
Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits. (1974) (14)
Ultracentrifuge Studies with a Synthetic Boundary Cell. III. Sedimentation of a Slow Component in the Presence of a Faster Species (1958) (14)
19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits. (1985) (14)
Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase. (1991) (14)
Quaternary constraint in hybrid of aspartate transcarbamylase containing wild-type and mutant catalytic subunits. (1975) (13)
Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase. (1987) (13)
Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli. (1981) (13)
Aspartate transcarbamoylase (Escherichia coli): preparation of subunits. (1978) (13)
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. (1991) (13)
Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge (1971) (13)
Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge (1971) (13)
Kinetics of the interaction of N-(phosphonacetyl)-L-aspartate with the catalytic subunit of aspartate transcarbamoylase. A slow conformational change subsequent to binding. (1986) (13)
Genetic characterization of the folding domains of the catalytic chains in aspartate transcarbamoylase. (1983) (13)
The mechanism of dissociation of aspartate transcarbamoylase by p-mercuribenzoate. (1981) (12)
Particle Size Determination of Colloidal Systems by the Supercentrifuge. (1940) (12)
Attenuation in the regulation of the pyrBI operon in Escherichia coli. In vivo studies of transcriptional termination. (1989) (12)
Primary structure and properties of an inactive mutant aspartate transcarbamoylase. (1979) (12)
Communication between dissimilar subunits in aspartate transcarbamoylase: effect of inhibitor and activator on the conformation of the catalytic polypeptide chains. (1979) (12)
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. (1991) (12)
Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase. (1992) (11)
Purification and characterization of a mutant aspartate transcarbamoylase lacking enzyme activity. (1979) (11)
Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase. (1992) (11)
From allostery to mutagenesis: 20 years with aspartate transcarbamoylase. (1987) (11)
In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains (1993) (11)
Peptide‐protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase (1993) (10)
A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits. (1980) (10)
Boundary spreading in sedimentation velocity experiments on partially liganded aspartate transcarbamoylase. A ligand-mediated isomerization. (1989) (10)
Physical-chemical studies on deoxyribonucleic acid; a discussion. (1957) (10)
Viscosity studies on the association of tobacco mosaic virus. (1947) (10)
Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits. (1992) (10)
13C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate. (1992) (10)
The Physical Properties of Infective Particles (1959) (10)
Measurement of partial specific volume by sedimentation equilibrium in H2O-D2O solutions. (1973) (10)
The Effect of Pressure on Sedimentation, and Compressibility Measurements in the Ultracentrifuge1 (1955) (9)
Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylase. (1977) (9)
IV – Sedimentation Velocity (1959) (9)
Cooperative interactions in hybrids of aspartate transcarbamylase containing succinylated regulatory polypeptide chains. (1975) (9)
Communication between polypeptide chains in aspartate transcarbamoylase. Conformational changes at the active sites of unliganded chains resulting from ligand binding to other chains. (1986) (9)
Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Implications for domain switching (1996) (9)
Still looking for the Ivory Tower. (2000) (9)
Structure, Function and Dynamics of a Regulatory Enzyme — Aspartate Transcarbamylase (1972) (9)
Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains (1993) (9)
Analysis of association-dissociation equilibria in proteins by difference and differential sedimentation. (1973) (8)
The contribution of threonine 55 to catalysis in aspartate transcarbamoylase. (1992) (8)
Communication between subunits in aspartate transcarbamoylase. Effect of active site ligands on the tertiary structure of regulatory chains. (1981) (8)
pryB mutations as suppressors of arginine auxotrophy in Salmonella typhimurium (1980) (8)
Alignment of Schlieren and Rayleigh opitcal systems in the ultracentrifuge. 3. Design, construction, and placement of Rayleigh mask. (1972) (8)
Ligand-promoted strengthening of interchain bonding domains in catalytic subunits of aspartate transcarbamoylase. (1982) (7)
A difference sedimentation equilibrium technique for measuring small changes in molecular weight. II. Experimental. (1974) (7)
Spectral alterations associated with the ligand-promoted gross conformational change in aspartate transcarbamoylase. (1981) (7)
The influence of quaternary structure on the active site of an oligomeric enzyme. Catalytic subunit of aspartate transcarbamoylase. (1984) (7)
Determination of sedimentation constants in the Sharples supercentrifuge. (1948) (7)
Linkage between reactivity of sulfhydryl groups and subunit interactions in aspartate transcarbamoylase. (1982) (7)
The isolation and characterization of a macro-molecular ribonucleoprotein from yeast. (1956) (6)
Association of the catalytic subunit of aspartate transcarbamoylase with a zinc‐containing polypeptide fragment of the regulatory chain leads to increases in thermal stability (1994) (6)
19F nuclear magnetic resonance studies of communication between catalytic and regulatory subunits in aspartate transcarbamoylase. (1985) (6)
Crystallization and preliminary X-ray diffraction studies of an inactive mutant aspartate transcarbamoylase from Escherichia coli. (1981) (5)
A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains. (1996) (5)
Mechanism of disproportionation of asparate transcarbamoylase molecules lacking one regulatory subunit. (1980) (5)
Asparate transcarbamoylase: Current opinion in structural biology 1993, 3:960–967 (1993) (5)
Deductions from hydrodynamic and thermodynamic measurements. (1960) (5)
A difference sedimentation equilibrium technique for measuring small changes in molecular weight. I. Theory and computer simulation. (1974) (5)
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 (1994) (4)
Assembly of Aspartate Transcarbamoylase in Escherichia colia (1983) (4)
On conformational changes in the regulatory enzyme aspartate transcarbamoylase. (1985) (4)
VII – Interpretation of Sedimentation Data (1959) (4)
Advances in Virus Research. Vol. I. (1954) (4)
Preliminary Results on the Crystal and Molecular Structure of Native and Mutant Aspartate Carbamoyltransferase at Neutral pH (1988) (3)
Quantitative urea gradient gel electrophoresis for studies of dissociation and unfolding of oligomeric proteins. (2002) (3)
V – The Transient States during the Approach to Sedimentation Equilibrium (1959) (3)
AN ALIGNMENT CHART FOR THE COMPUTATION OF ULTRACENTRIFUGATION RESULTS (1942) (3)
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation (2006) (3)
VI – Sedimentation Equilibrium (1959) (3)
Assembly of aspartate transcarbamoylase in Escherichia coli. (1983) (2)
II – General Considerations (1959) (2)
Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coli. (1984) (2)
Optical Systems for Sedimentation Analysis (1963) (2)
1H NMR studies on the catalytic subunit of aspartate transcarbamoylase. (1992) (2)
Assembly of catalytic subunits of aspartate transcarbamoylase from Escherichia coli. (1980) (2)
Physical techniques in biological research. Vol. II. Physical chemical techniques: Edited by Gerald Oster and Arthur W. Pollister. Academic Press Inc., New York, N. Y., 1956. 502 pp. Price $12.80 (1957) (1)
Structure and properties of nucleic acids and nucleoproteins. An informal discussion (1954) (1)
Those wonderful early years with the Model E ultracentrifuge and David Yphantis. (2004) (1)
Remembering Bill Harrington (1993) (1)
Formation of Active Aspartate Transcarbamoylase from Defective Polypeptide Chains Produced by Site-Directed Mutagenesis (1988) (1)
22 Impact of Regulations on the Conduct of Research (2001) (1)
Ultracentifugation in biochemistry (2016) (1)
Donnan effect as measured by sedimentation equilibrium for the protein cytochrome c (1978) (1)
volume and a given surface area. It follows, then. that the ratio p represents at (1964) (0)
The ultracentrifuge: A retrospective and prospective view (1980) (0)
Differential Scanning Calorimetry of Aspartate Transcarbamoylase and Its Isolated Subunits * (2002) (0)
On scientific freedom and responsibility. (2002) (0)
Sulfur in proteins: Proceedings of a symposium held at Falmouth, Massachusetts, May 1958: Edited by R. Beneschet al. Academic Press Inc., New York and London, 1959. xi + 469 pp. Price $14.00 (1960) (0)
Synthesis of aspartate transcarbam Transcriptional regulation of the pnh (2016) (0)
Summary Remarks: A Retrospect on Proteins (1979) (0)
STRUCTURE OF THE R105A MUTANT CATALYTIC TRIMER OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE AT 2.0-A RESOLUTION (2002) (0)
ACID: AN INTERRUPTED TWO-STRAND MODEL* (2016) (0)
Letter from Howard K. Schachman to Joshua Lederberg (1971) (0)
III – Experimental Aspects (1959) (0)
Advances in Virus Research. Volume II. (1955) (0)
A retrospect on proteins. (1979) (0)

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