J. Manning

发表

Hemoglobin Jamaica plain--a sickling hemoglobin with reduced oxygen affinity.

E. Neufeld, Yuxun Zhang, Alon Geva, 2004, The New England journal of medicine.

Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities.

A. Scaloni, F. Bossa, O. Schneewind, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Dietary polyunsaturated fat decreases interaction between low density lipoproteins and arterial proteoglycans

A. Gebre, J. Parks, L. Rudel, 1994, Lipids.

Recombinant sickle hemoglobin containing a lysine substitution at Asp-85(alpha): expression in yeast, functional properties, and participation in gel formation.

J. Himanen, A. Popowicz, J. Manning, 1997, Blood.

Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding.

L. R. Manning, B. Chait, J. Padovan, 2017, Analytical biochemistry.

Production of the biotechnologically relevant AFP from Aspergillus giganteus in the yeast Pichia pastoris.

J. Gavilanes, Á. Martínez-del-Pozo, B. San Segundo, 2010, Protein expression and purification.

Recombinant human sickle hemoglobin expressed in yeast.

O. Schneewind, J. J. Martín de Llano, J. Manning, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Embryonic and Fetal Human Hemoglobins: Structures, Oxygen Binding, and Physiological Roles.

L. R. Manning, B. Chait, J. Padovan, 2020, Sub-cellular biochemistry.

Gas chromatographic determination of the carbamylation of hemoglobin S by cyanate.

A. Cerami, C. K. Lee, P. Gillette, 1973, The Journal of laboratory and clinical medicine.

Determination of D- and L-amino acids by ion exchange chromatography as L-D and L-L dipeptides.

S. Moore, J. Manning, 1968, The Journal of biological chemistry.

Determination of D- and L-amino acid residues in peptides. Use of tritiated hydrochloric acid to correct for racemization during acid hydrolysis.

J. Manning, 1970, Journal of the American Chemical Society.

Enzyme-Activated Inhibitors of Bacterial D-Amino Acid Transaminase as Antimicrobial Agents

M. Merola, H. Ueno, J. Manning, 1987 .

Interaction of gamma-glutamyl transpeptidase with acivicin.

A. Meister, T. Smith, J. Manning, 1994, The Journal of biological chemistry.

Identification of L-methionine S-sulfoximine as the diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase.

A. Meister, J. Manning, W. B. Rowe, 1969, Biochemistry.

D-CYCLOSERINE INACTIVATION OF D-AMINO ACID AMINOTRANSFERASE LEADS TO A STABLE NONCOVALENT PROTEIN COMPLEX WITH AN AROMATIC CYCLOSERINE-PLP DERIVATIVE

G. Petsko, D. Ringe, D. Peisach, 1998 .

Fatty acid composition of low-density lipoprotein influences its susceptibility to autoxidation.

L. Rudel, M. Thomas, J. Manning, 1994, Biochemistry.

Reactivity of the amino groups of carbonmonoxyhemoglobin S with glyceraldehyde.

A. Acharya, J. Manning, 1980, The Journal of biological chemistry.

Some factors that influence the nonenzymatic glycation of peptides and polypeptides by glyceraldehyde

H. Ueno, J. Manning, Yasuo Bai, 1989, Journal of protein chemistry.

Sequence-dependent reactivity of model peptides with glyceraldehyde.

H. Ueno, Y. Bai, N. Mori, 1989, Carbohydrate research.

Inhibition of erythrocyte sickling in vitro by DL-glyceraldehyde.

J. Manning, A. M. Nigen, 1977, Proceedings of the National Academy of Sciences of the United States of America.

Studies on the Amadori rearrangement in a model system: chromatographic isolation of intermediates and product.

N. Mori, J. Manning, 1986, Analytical biochemistry.

Schiff base adducts of glyceraldehyde with hemoglobin. Differences in the Amadori rearrangement at the alpha-amino groups.

A. Acharya, J. Manning, L. Sussman, 1983, The Journal of biological chemistry.

Amadori rearrangement of glyceraldehyde-hemoglobin Schiff base adducts. A new procedure for the determination of ketoamine adducts in proteins.

A. Acharya, J. Manning, 1980, The Journal of biological chemistry.

Nano Gel Filtration Reveals How Fish Hemoglobins Release Oxygen: The Root Effect.

L. R. Manning, J. Manning, 2020, Analytical biochemistry.

Developmental expression of human hemoglobins mediated by maturation of their subunit interfaces

L. R. Manning, B. Chait, J. Padovan, 2010, Protein science : a publication of the Protein Society.

The acetylation state of human fetal hemoglobin modulates the strength of its subunit interactions: long-range effects and implications for histone interactions in the nucleosome.

L. R. Manning, J. Manning, James M. Manning, 2001, Biochemistry.

Exchange of Subunit Interfaces between Recombinant Adult and Fetal Hemoglobins

L. R. Manning, R. Winslow, W. Jenkins, 1997, The Journal of Biological Chemistry.

Transposing sequences between fetal and adult hemoglobins indicates which subunits and regulatory molecule interfaces are functionally related.

L. R. Manning, B. Chait, O. Platt, 2000, Biochemistry.

N‐terminal acetylation and protonation of individual hemoglobin subunits: Position‐dependent effects on tetramer strength and cooperativity

L. R. Manning, B. Chait, J. Padovan, 2005, Protein science : a publication of the Protein Society.

beta-elimination of beta-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reaction.

J. Manning, T. S. Soper, 1978, Biochemistry.

Kinetics of the carbamylation of the amino groups of sickle cell hemoglobin by cyanate.

C. K. Lee, J. Manning, 1973, The Journal of biological chemistry.

Systematic enhancement of polymerization of recombinant sickle hemoglobin mutants: implications for transgenic mouse model for sickle cell anemia.

B. Chait, U. Mirza, J. Manning, 1997, Blood.

Substrate-induced changes in sulfhydryl reactivity of bacterial D-amino acid transaminase.

H. Ueno, J. Manning, T. S. Soper, 1985, Archives of biochemistry and biophysics.

Subunit dissociations in natural and recombinant hemoglobins

L. R. Manning, K. Vandegriff, R. Winslow, 1996, Protein science : a publication of the Protein Society.

Mouse peritoneal macrophages release leukotriene C in response to a phagocytic stimulus.

C. Rouzer, Z. Cohn, P. Blackburn, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Phosphorylation of Serine Induces Lysine p Ka Increases in Histone N-Termini and Signaling for Acetylation. Transcription Implications.

L. R. Manning, J. Manning, 2018, Biochemistry.

Remote contributions to subunit interactions: lessons from adult and fetal hemoglobins.

L. R. Manning, B. Chait, J. Padovan, 1999, Trends in biochemical sciences.

Oxygenation in tumors by modified hemoglobins

L. R. Manning, R. Jain, M. Nozue, 1996, Journal of surgical oncology.

Design of Chemically Modified and Recombinant Hemoglobins as Potential Red Cell Substitutes

J. Manning, 1995 .

Preparation, properties, and plasma retention of human hemoglobin derivatives: comparison of uncrosslinked carboxymethylated hemoglobin with crosslinked tetrameric hemoglobin.

L. R. Manning, B. Chait, R. Winslow, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Influence of ligation state and concentration of hemoglobin A on its cross-linking by glycolaldehyde: functional properties of cross-linked, carboxymethylated hemoglobin.

L. R. Manning, J. Manning, 1988, Biochemistry.

Preparation of hemoglobin carbamylated at specific NH2-terminal residues.

J. Manning, 1981, Methods in enzymology.

Chromatographic determination of the D- and L-amino acid residues in pneumococcal C-polysaccharide.

J. Manning, 1971, The Journal of biological chemistry.

Sickle Hemoglobin Polymer Stability Probed by Triple and Quadruple Mutant Hybrids*

R. Josephs, F. Ferrone, J. Manning, 2002, The Journal of Biological Chemistry.

Participation and Strength of Interaction of Lysine 95(β) in the Polymerization of Hemoglobin S as Determined by Its Site-directed Substitution by Isoleucine (*)

B. Chait, K. Schneider, J. Himanen, 1995, The Journal of Biological Chemistry.

A recombinant human hemoglobin with asparagine‐102(β) substituted by alanine has a limiting low oxygen affinity, reduced marginally by chloride

L. R. Manning, K. Vandegriff, R. Winslow, 1995, Protein science : a publication of the Protein Society.

Properties of a recombinant human hemoglobin double mutant: Sickle hemoglobin with Leu‐88 (β) at the primary aggregation site substituted by Ala

J. Manning, J. De Llano, 1994, Protein science : a publication of the Protein Society.

Biochemical and functional properties of recombinant human sickle hemoglobin expressed in yeast.

B. Chait, K. Schneider, J. J. Martín de Llano, 1993, The Journal of biological chemistry.

An improved process for the production of sterile modified haemoglobin solutions.

J. Hess, M. Chavez, R. Berger, 1997, Biologicals : journal of the International Association of Biological Standardization.

Effects of D-serine on bacterial D-amino acid transaminase: accumulation of an intermediate and inactivation of the enzyme.

G. Petsko, B. Stoddard, D. Ringe, 1989, Biochemistry.

Increased survival of sickle-cell erythrocytes after treatment in vitro with sodium cyanate.

A. Cerami, P. Gillette, J. Manning, 1971, Proceedings of the National Academy of Sciences of the United States of America.

The reaction of beta-chloroglutamic acid with glutamate-aspartate transaminase.

P. Fasella, J. Manning, R. Khomutov, 1968, European journal of biochemistry.

Studies on the mechanism of activation acid beta-decarboxylase by alpha-keto acids and pyridoxal 5'-phosphate.

A. Meister, J. Manning, J. Nishimura, 1962, Biochemistry.

Determining subunit dissociation constants in natural and recombinant proteins.

L. R. Manning, R. Winslow, W. Jenkins, 1999, Methods in enzymology.

Properties of a recombinant human hemoglobin with aspartic acid 99 (β), an important intersubunit contact site, substituted by lysine

L. R. Manning, B. Chait, K. Vandegriff, 1994, Protein science : a publication of the Protein Society.

Nucleation and polymerization of sickle hemoglobin with Leu beta 88 substituted by Ala.

F. Ferrone, J. Himanen, J. J. Martín de Llano, 1997, Journal of molecular biology.

Inactivation of pyridoxal phosphate enzymes by gabaculine. Correlation with enzymic exchange of beta-protons.

J. Manning, T. S. Soper, 1982, The Journal of biological chemistry.

Covalent inhibitors of the gelation of sickle cell hemoglobin and their effects on function.

J. Manning, 1991, Advances in enzymology and related areas of molecular biology.

Properties of carboxymethylated cross-linked hemoglobin A.

L. R. Manning, W. Fantl, H. Ueno, 1987, Biochemistry.

Normal and Abnormal Protein Subunit Interactions in Hemoglobins*

L. R. Manning, J. Manning, Xianfeng Li, 1998, The Journal of Biological Chemistry.

Purification and characterization of recombinant human sickle hemoglobin expressed in yeast.

O. Schneewind, J. J. Martín de Llano, J. Manning, 1994, Methods in Enzymology.

Carboxyalkylated Hemoglobin as a Potential Blood Substitute.

J. Manning, 1987 .

Determination of free D-amino acids with a bacterial transaminase: their depletion leads to inhibition of bacterial growth.

D. Ringe, K. Soda, J. Manning, 1994, Analytical biochemistry.

Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro.

Susan Jones, Sheena E Radford, James Manning, 2003, Journal of molecular biology.

Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase.

D. Ringe, D. Peisach, D. Chipman, 1998, Biochemistry.

The ubiquitous cofactor NADH protects against substrate‐induced inhibition of a pyridoxal enzyme

G. Petsko, D. Ringe, K. Soda, 1996, Protein science : a publication of the Protein Society.

Characterization of a novel cysteine-rich antifungal protein from Fusarium graminearum with activity against maize fungal pathogens.

A. Di Pietro, Á. Martínez-del-Pozo, M. Roncero, 2018, International journal of food microbiology.

Reaction of glycolaldehyde with proteins: latent crosslinking potential of alpha-hydroxyaldehydes.

A. Acharya, J. Manning, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Inactivation of bacterial D-amino acid transaminases by the olefinic amino acid D-vinylglycine.

C. Walsh, P. Marcotte, J. Manning, 1977, The Journal of biological chemistry.

Selective carboxymethylation of the alpha-amino groups of hemoglobin. Effect on functional properties.

A. Acharya, W. Fantl, J. Manning, 1983, The Journal of biological chemistry.

Labeling of hemoglobin with pyridoxal phosphate.

A. Acharya, R. Benesch, J. Manning, 1982, The Journal of biological chemistry.

Potassium cyanate as an inhibitor of the sickling of erythrocytes in vitro.

A. Cerami, J. Manning, 1971, Proceedings of the National Academy of Sciences of the United States of America.

Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine.

S. Futaki, K. Soda, K. Tanizawa, 1991, Biochemistry.

D-Glutamate-D-amino acid transaminase from bacteria.

H. Ueno, J. Manning, W. Jones, 1985, Methods in enzymology.

Studies on the mechanism of action of D-amino acid transaminase

J. Manning, 1994 .

Inhibition of Bacterial Growth by ,3-Chloro-D-Alanine

E. Gotschlich, J. Manning, W. Jones, 2022 .

Carbamylation of the chains of hemoglobin S by cyanate in vitro and in vivo.

R. Williams, P. Gillette, J. Manning, 1973, The Journal of biological chemistry.

Role reversal for substrates and inhibitors. Slow inactivation of D-amino acid transaminase by its normal substrates and protection by inhibitors.

D. Ringe, K. Soda, T. Yoshimura, 1993, The Journal of biological chemistry.

Covalent Chemical Modifiers of Sickle Cell Hemoglobin a

H. Ueno, J. Manning, Yasuo Bai, 1989, Annals of the New York Academy of Sciences.

Studies on the mechanism of action of cyanate in sickle cell disease. Oxygen affinity and gelling properties of hemoglobin S carbamylated on specific chains.

C. K. Lee, J. Manning, N. Njikam, 1974, The Journal of biological chemistry.

N‐terminal contributions of the γ‐subunit of fetal hemoglobin to its tetramer strength: Remote effects at subunit contacts

B. Chait, J. Padovan, T. Yagami, 2002, Protein science : a publication of the Protein Society.

Intrinsic regulation of hemoglobin expression by variable subunit interface strengths

L. R. Manning, B. Chait, J. Padovan, 2012, The FEBS journal.

Energetic differences at the subunit interfaces of normal human hemoglobins correlate with their developmental profile.

L. R. Manning, R. Manning, J. Padovan, 2009, Biochemistry.

Human embryonic, fetal, and adult hemoglobins have different subunit interface strengths. Correlation with lifespan in the red cell

L. R. Manning, B. Chait, J. Padovan, 2007, Protein science : a publication of the Protein Society.

Human acylpeptide hydrolase. Studies on its thiol groups and mechanism of action.

A. Scaloni, D. Barra, J. Manning, 1994, The Journal of biological chemistry.

Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase.

A. Scaloni, S. Remington, M. Feese, 1993, Journal of molecular biology.

Deficiency of acylpeptide hydrolase in small-cell lung carcinoma cell lines.

A. Scaloni, F. Bossa, O. Schneewind, 1992, The Journal of laboratory and clinical medicine.

[2] Determination of d- and l-amino acids by ion-exchange chromatography.

J. Manning, 1972, Methods in enzymology.

The effects of cyanate in vitro on red blood cell metabolism and function in sickle cell anemia.

A. Cerami, D. Miller, J. Manning, 1972, The Journal of clinical investigation.

Adherence of Vancomycin to Proteins

J. Manning, K. Kishimoto, 2001, Journal of protein chemistry.

Specifically carboxymethylated hemoglobin as an analogue of carbamino hemoglobin. Solution and X-ray studies of carboxymethylated hemoglobin and X-ray studies of carbamino hemoglobin.

W. Fantl, P. Rogers, A. Arnone, 1987, The Journal of biological chemistry.

Stereospecificity of reactions catalyzed by bacterial D-amino acid transaminase.

D. Ringe, K. Soda, K. Tanizawa, 1989, The Journal of biological chemistry.

Catalytic ability and stability of two recombinant mutants of D‐amino acid transaminase involved in coenzyme binding

G. Petsko, D. Ringe, D. Peisach, 1995, Protein science : a publication of the Protein Society.

Production enzymatique de d-amino acides

J. Manning, A. Pozo, 1990 .

Chiral discrimination among aminotransferases: inactivation by 4-amino-4,5-dihydrothiophenecarboxylic acid.

D. Ringe, R. Silverman, Dali Liu, 2010, Biochemistry.

Studies on an Active Site residue, E177, That Affects Binding of the Coenzyme in D-Amino Acid Transaminase, and Mechanistic Studies on a Suicide Substrate

D. Ringe, J. Manning, B. W. Lepore, 2000 .

Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.

G. Petsko, D. Ringe, K. Soda, 1995, Biochemistry.

Kinetic and stereochemical comparison of wild-type and active-site K145Q mutant enzyme of bacterial D-amino acid transaminase.

D. Ringe, S. Futaki, K. Soda, 1993, Journal of Biological Chemistry.

Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5'-phosphate.

D. Ringe, K. Soda, T. Yoshimura, 1992, Biochemistry.

Inactivation of dimeric D-amino acid transaminase by a normal substrate through formation of an unproductive coenzyme adduct in one subunit.

D. Ringe, S. Futaki, K. Soda, 1992, Biochemistry.

Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase. Effects of exogenous amines on the slow formation of intermediates.

B. Stoddard, D. Ringe, S. Futaki, 1990, Journal of Biological Chemistry.

Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase.

H. Tanaka, K. Tanizawa, M. Merola, 1989, Biochemistry.

Inactivation of bacterial D-amino acid transaminase by beta-chloro-D-alanine.

J. Manning, W. Jones, T. S. Soper, 1977, Journal of Biological Chemistry.

Inhibition of bacterial growth by beta-chloro-D-alanine.

E. Gotschlich, J. Manning, W. Jones, 1974, Proceedings of the National Academy of Sciences of the United States of America.

Site-specific modification of hemoglobin by methyl acetyl phosphate.

H. Ueno, R. Kluger, J. Manning, 1986, Archives of biochemistry and biophysics.

Compensation for D-glutamate auxotrophy of Escherichia coli WM335 by D-amino acid aminotransferase gene and regulation of murI expression.

K. Endo, K. Soda, L. Liu, 1998, Bioscience, biotechnology, and biochemistry.

Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.

D. Ringe, D. Peisach, K. Soda, 1999, Biochemistry.

Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: isolation and initial characterization of a pyridoxo intermediate related to inactivation.

G. Petsko, B. Chait, D. Ringe, 1998, Biochemistry.

Enzyme-activated inhibition of bacterial D-amino acid transaminase by beta-cyano-D-alanine.

H. Ueno, J. Manning, T. S. Soper, 1984, Biochemical and biophysical research communications.

Methyl acetyl phosphate as a covalent probe for anion-binding sites in human and bovine hemoglobins.

H. Ueno, J. Manning, M. Pospischil, 1989, The Journal of biological chemistry.

Acetylenic-γ-aminobutyrate as an enzyme-activated inhibitor of D-amino acid transaminase

M. Merola, H. Ueno, J. Manning, 1989 .

Biochemical and Physiological Properties of Carbamylated Hemoglobin S

A. Cerami, D. Miller, P. Gillette, 1974 .

Structural Investigations on Human Erythrocyte Acylpeptide Hydrolase by Mass Spectrometric Procedures

A. Scaloni, G. Marino, A. Andolfo, 1999, Journal of protein chemistry.

Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme.

L. R. Manning, A. Scaloni, D. Barra, 1992, The Journal of biological chemistry.

Acylpeptide hydrolase activity from erythrocytes.

J. Manning, W. Jones, 1985, Biochemical and biophysical research communications.

Oxygen-linked binding sites for inorganic anions to hemoglobin.

J. O. Alben, J. Manning, A. M. Nigen, 1980, The Journal of biological chemistry.

Examples of chemical modification and recombinant DNA approaches with hemoglobin.

J. Manning, 1996, Transfusion clinique et biologique : journal de la Societe francaise de transfusion sanguine.

Random chemical modification of hemoglobin to identify chloride binding sites in the central dyad axis: their role in control of oxygen affinity.

J. Manning, 1994, Artificial cells, blood substitutes, and immobilization biotechnology.

Reversible dissociation/association of D-amino acid transaminase subunits: properties of isolated active dimers and inactive monomers.

J. Manning, K. Kishimoto, C. Yasuda, 2000, Biochemistry.

The N-terminal Sequence Affects Distant Helix Interactions in Hemoglobin

L. R. Manning, B. Chait, R. Winslow, 1998, The Journal of Biological Chemistry.

Low‐Dose Contraceptive Estrogen‐Progestin and Coronary Artery Atherosclerosis of Monkeys

J. Parks, M. Anthony, M. Adams, 2000, Obstetrics and gynecology.

Reactivity of cyanate with valine-1 (alpha) of hemoglobin. A probe of conformational change and anion binding.

J. Manning, B. D. Bass, A. M. Nigen, 1976, The Journal of biological chemistry.

The interaction of anions with hemoglobin carbamylated on specific NH2-terminal residues.

J. Manning, A. M. Nigen, 1975, The Journal of biological chemistry.

Substrate specificity of an acylaminopeptidase that catalyzes the cleavage of the blocked amino termini of peptides.

J. Manning, W. Jones, 1988, Biochimica et biophysica acta.

Different modes of action of inhibitors of bacterial D-amino acid transaminase. A target enzyme for the design of new antibacterial agents.

J. Manning, T. S. Soper, 1981, Journal of Biological Chemistry.

A Recombinant Sickle Hemoglobin Triple Mutant with Independent Inhibitory Effects on Polymerization*

B. Chait, J. Himanen, U. Mirza, 1996, The Journal of Biological Chemistry.

Enhanced survival of sickle erythrocytes upon treatment with glyceraldehyde.

J. Manning, L. J. Benjamin, 1986, Blood.

Inhibition of deoxyhemoglobin S polymerization by glyceraldehyde.

A. Acharya, J. Manning, W. Jones, 1984, Analytical biochemistry.

Effects of glyceraldehyde on the structural and functional properties of sickle erythrocytes.

J. Manning, A. M. Nigen, 1978, The Journal of clinical investigation.

Enzymic cleavage of the blocked amino terminal residues of peptides.

L. R. Manning, J. Manning, W. Jones, 1986, Biochemical and biophysical research communications.

Selectivity in the modification of the alpha-amino groups of hemoglobin on reductive alkylation with aliphatic carbonyl compounds. Influence of derivatization on the polymerization of hemoglobin S.

A. Acharya, J. Manning, L. Sussman, 1985, The Journal of biological chemistry.

Histidine decarboxylase of Lactobacillus 30a: inactivation and active-site labeling by L-histidine methyl ester.

R. Lane, J. Manning, E. Snell, 1976, Biochemistry.

Influence of trifluoroacetic acid on retention times of histidine-containing tryptic peptides in reverse phase HPLC.

B. Manjula, A. Acharya, V. Fischetti, 2009, International journal of peptide and protein research.

Activity and spectroscopic properties of bacterial D-amino acid transaminase after multiple site-directed mutagenesis of a single tryptophan residue.

D. Ringe, H. Tanaka, K. Soda, 1989, Biochemistry.

Kinetic study of the interaction between aspartate aminotransferase and threo-beta-chloroglutamate.

M. Brunori, P. Fasella, E. Antonini, 1970, Biochemistry.

A Cross-Sectional Analysis of IWU MBA Graduates and Current Students: Is there a change in the frequency in which transformational leadership behaviors are regularly demonstrated?

J. Manning, 2010 .

Nitric oxide can modify amino acid residues in proteins.

L. R. Manning, M. Moriguchi, J. Manning, 1992, Biochemical and biophysical research communications.

Solubility of sickle hemoglobin measured by a kinetic micromethod.

F. Ferrone, J. Himanen, J. J. Martín de Llano, 1996, Biophysical journal.

350: TORQUE ACCELERATION ENERGY AS AN ALTERNATIVE PREDICTOR OF ANAEROBIC POWER

S. Lephart, D. Perrin, E. Saliba, 1987 .

contact site, substituted by lysine

B. Chait, K. Vandegriff, R. Winslow, 1994 .

Mutational analysis of sickle haemoglobin (Hb) gelation

B. Chait, J. Padovan, J. Himanen, 1999, Biotechnology and applied biochemistry.

Human Erythrocyte Membrane Band 3 Protein Influences Hemoglobin Cooperativity

L. R. Manning, O. Platt, Yuxun Zhang, 2003, Journal of Biological Chemistry.

Contributions to nucleosome dynamics in chromatin from interactive propagation of phosphorylation/acetylation and inducible histone lysine basicities

L. R. Manning, J. Manning, 2018, Protein science : a publication of the Protein Society.

MAJOR SITES FOR THE OXYGEN-LINKED BINDING OF CHLORIDE TO HEMOGLOBIN

S. Charache, J. O. Alben, J. Manning, 1978 .

INHIBITION OF ERYTHROCYTE SICKLING IN VITRO BY GLYCERALDEHYDE 1

J. Manning, A. M. Nigen, 1978 .

Unique stereospecificity of D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase for C-4' hydrogen transfer of the coenzyme

H. Kagamiyama, K. Soda, T. Yoshimura, 1993 .