H. Rubin

发表

Function of the Cytochrome bc1-aa3 Branch of the Respiratory Network in Mycobacteria and Network Adaptation Occurring in Response to Its Disruption

R. Coppel, Assunta Pelosi, V. Mizrahi, 2005, Journal of bacteriology.

Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis.

W. T. Moore, C. Lukacs, J. Lambris, 1996, Biochemistry.

Antichymotrypsin interaction with chymotrypsin. Partitioning of the complex.

E. Rescorla, B. Cooperman, E. Stavridi, 1993, The Journal of biological chemistry.

Distortion of the active site of chymotrypsin complexed with a serpin.

L. Mayne, M. Plotnick, H. Rubin, 1996, Biochemistry.

Structural Change in α-Chymotrypsin Induced by Complexation with α1-Antichymotrypsin As Seen by Enhanced Sensitivity to Proteolysis†

John D Lambris, W. T. Moore, C. Lukacs, 1996 .

Discovery of Imidazo[1,2-a]pyridine Ethers and Squaramides as Selective and Potent Inhibitors of Mycobacterial Adenosine Triphosphate (ATP) Synthesis.

Christopher B. Cooper, Amit K. Gupta, D. Murray, 2017, Journal of medicinal chemistry.

Role of small t antigen in the acute transforming activity of SV40

D. Livingston, J. Figge, H. Rubin, 1982, Cell.

High level expression of the large subunit of mouse ribonucleotide reductase in a baculovirus system

B. Cooperman, H. Rubin, C. Scott, 1993, FEBS letters.

Comparison of translation in eukaryotic mode with translation in prokaryote mode.

H. Rubin, M. Halim, 1992, Journal of theoretical biology.

The Stringent Response of Mycobacterium tuberculosis Is Required for Long-Term Survival

V. Mizrahi, C. Barry, H. Rubin, 2000, Journal of bacteriology.

Erratum to: “Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis”

H. Rubin, J. Salem, D. Avarbock, 1999 .

Scaffold morphing leading to evolution of 2,4-diaminoquinolines and aminopyrazolopyrimidines as inhibitors of the ATP synthesis pathway

Amit K. Gupta, G. Balakrishnan, A. Narayan, 2016 .

Evidence that the 5' end of rabbit globin mRNA is hybridized with its 3' end.

H. Rubin, M. Halim, R. Stefanko, 1994, The International journal of biochemistry.

Patents and literature

R. Brent, R. Hochstrasser, A. Goldberg, 1990 .

Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions.

S. Lessin, H. Rubin, Z. M. Wang, 1994, Journal of immunology.

Inhibition of human neutrophil superoxide generation by alpha 1-antichymotrypsin.

B. Cooperman, S. Douglas, J. Johnson, 1991, Journal of immunology.

Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins.

B. Cooperman, J. Johnson, H. Rubin, 1990, The Journal of biological chemistry.

Differential Sensitivity of the Tyrosyl Radical of Mouse Ribonucleotide Reductase to Nitric Oxide and Peroxynitrite*

H. Rubin, Y. Henry, J. Salem, 1998, The Journal of Biological Chemistry.

Alzheimer’s Peptide Aβ1–42 Binds to Two β-Sheets of α1-Antichymotrypsin and Transforms It from Inhibitor to Substrate*

C. Lukacs, H. Rubin, S. Janciauskiene, 1998, The Journal of Biological Chemistry.

The Control of Neutrophil Chemotaxis by Inhibitors of Cathepsin G and Chymotrypsin (*)

R. Stockley, D. Lomas, R. Carrell, 1995, The Journal of Biological Chemistry.

Limited proteolysis of Cl‐inhibitor by chymotrypsin‐like proteinases

B. Cooperman, H. Rubin, O. Schoenberger, 1989, FEBS letters.

The biology and biochemistry of antichymotrypsin and its potential role as a therapeutic agent.

H. Rubin, 1992, Biological chemistry Hoppe-Seyler.

Reaction of human skin chymotrypsin-like proteinase chymase with plasma proteinase inhibitors.

B. Cooperman, H. Rubin, G. Lazarus, 1989, The Journal of biological chemistry.

Role of the P6-P3' region of the serpin reactive loop in the formation and breakdown of the inhibitory complex.

M. Plotnick, H. Rubin, Z. M. Wang, 1997, Biochemistry.

Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties.

B. Cooperman, H. Rubin, Z. M. Wang, 1993, The Journal of biological chemistry.

Recombinant Expression of Human Mast Cell Proteases Chymase and Tryptase

T. Selwood, H. Rubin, N. Schechter, 1998, Biological chemistry.

Production of active recombinant human chymase from a construct containing the enterokinase cleavage site of trypsinogen in place of the native propeptide sequence.

H. Rubin, Z. M. Wang, N. Schechter, 1995, Biological chemistry Hoppe-Seyler.

The carboxyl terminus heptapeptide of the R2 subunit of mammalian ribonucleotide reductase inhibits enzyme activity and can be used to purify the R1 subunit

B. Cooperman, H. Rubin, R. Hirschmann, 1990, FEBS letters.

Characterization of two genes encoding the Mycobacterium tuberculosis ribonucleotide reductase small subunit

H. Rubin, M. Chua, F. Yang, 1997, Journal of bacteriology.

Isolation of ribonucleotide reductase from Mycobacterium tuberculosis and cloning, expression, and purification of the large subunit

H. Rubin, F. Yang, G. Lu, 1994, Journal of bacteriology.

Malaria and the cell cycle.

H. Rubin, T. Leete, 1996, Parasitology today.

Conformational change and intermediates in the unfolding of alpha 1-antichymotrypsin.

S. Bottomley, H. Rubin, M. Pearce, 2000, The Journal of biological chemistry.

An inhibitor(s) of globin mRNA translation in rabbit serum.

H. Rubin, M. Halim, R. Stefanko, 1991, The International journal of biochemistry.

Effect of serine proteinase inhibitors on neutrophil function: α‐1‐proteinase inhibitor, antichymotrypsin, and a recombinant hybrid mutant of antichymotrypsin (LEX032) modulate neutrophil adhesion interactions

H. Rubin, H. Sands, T. Hugli, 1998, Journal of leukocyte biology.

Conversion of alpha 1-antichymotrypsin into a human neutrophil elastase inhibitor: demonstration of variants with different association rate constants, stoichiometries of inhibition, and complex stabilities.

B. Cooperman, M. Plotnick, H. Rubin, 1994, Biochemistry.

Regulation of neutrophil superoxide by antichymotrypsin-chymotrypsin complexes.

P. Enriquez, B. Cooperman, H. Rubin, 1992, The Journal of biological chemistry.

Systematic analysis of conservation relations in Escherichia coli genome-scale metabolic network reveals novel growth media.

Calin Belta, Harvey Rubin, Marcin Imielinski, 2006, Biophysical journal.

A high-throughput small-molecule screen to identify a novel chemical inhibitor of Clostridium difficile.

Jun Zhu, H. Rubin, T. Yano, 2014, International journal of antimicrobial agents.

Crystal structure of the biologically active form of class Ib ribonucleotide reductase small subunit from Mycobacterium tuberculosis

U. Uhlin, H. Rubin, Jamaine S. Davis, 2004, FEBS letters.

The tyrosyl free radical of recombinant ribonucleotide reductase from Mycobacterium tuberculosis is located in a rigid hydrophobic pocket.

A. Barra, A. Gräslund, H. Rubin, 1998, Biochemistry.

Reduction of Clofazimine by Mycobacterial Type 2 NADH:Quinone Oxidoreductase

J. Winkler, H. Rubin, N. Schechter, 2010, The Journal of Biological Chemistry.

Characterization of thecydAB-Encoded Cytochrome bd Oxidase fromMycobacterium smegmatis

V. Mizrahi, B. Kana, S. Dawes, 2001, Journal of bacteriology.

Cysteine proteinases from distinct cellular compartments are recruited to phagocytic vesicles by Entamoeba histolytica.

Harvey Rubin, J. McKerrow, L. Brinen, 2002, Molecular and biochemical parasitology.

Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana--comparison with Escherichia coli and mouse.

M. Fontecave, H. Rubin, C. Gerez, 1998, European journal of biochemistry.

Nucleic Acid Metabolism

V. Mizrahi, H. Rubin, M. Buckstein, 2005 .

Inhibitors of type II NADH:menaquinone oxidoreductase represent a class of antitubercular drugs.

H. Rubin, E. Weinstein, J. Lonsdale, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Characterization of Nucleotide Pools as a Function of Physiological State in Escherichia coli

H. Rubin, M. Buckstein, Jian He, 2007, Journal of bacteriology.

Deficiency of the Novel Exopolyphosphatase Rv1026/PPX2 Leads to Metabolic Downshift and Altered Cell Wall Permeability in Mycobacterium tuberculosis

J. Bader, Dalin Rifat, P. Karakousis, 2015, mBio.

Calcium protects DNase I from proteinase K: a new method for the removal of contaminating RNase from DNase I.

H. Rubin, R. Tullis, 1980, Analytical biochemistry.

Alzheimer's peptide Abeta1-42 binds to two beta-sheets of alpha1-antichymotrypsin and transforms it from inhibitor to substrate.

C. Lukacs, H. Rubin, S. Janciauskiene, 1998, The Journal of biological chemistry.

Identification of Lysines within α1-Antichymotrypsin Important for DNA Binding. AN UNUSUAL COMBINATION OF DNA-BINDING ELEMENTS (*)

B. Cooperman, N. Naidoo, H. Rubin, 1995, The Journal of Biological Chemistry.

The Effects of Reactive Site Location on the Inhibitory Properties of the Serpin α1-Antichymotrypsin*

M. Plotnick, H. Rubin, N. Schechter, 2002, The Journal of Biological Chemistry.

Characterization of the type 2 NADH:menaquinone oxidoreductases from Staphylococcus aureus and the bactericidal action of phenothiazines.

R. Gennis, H. Rubin, T. Yano, 2014, Biochimica et biophysica acta.

A direct evidence for the involvement of poly(A) in protein synthesis.

H. Rubin, M. Halim, 1987, Biochemical and biophysical research communications.

Soybean Bowman-Birk protease inhibitor is a highly effective inhibitor of human mast cell chymase.

H. Rubin, N. Schechter, X. Wan, 1997, Archives of biochemistry and biophysics.

Stringent Response Factors PPX1 and PPK2 Play an Important Role in Mycobacterium tuberculosis Metabolism, Biofilm Formation, and Sensitivity to Isoniazid In Vivo

T. Wu, P. Karakousis, H. Rubin, 2016, Antimicrobial Agents and Chemotherapy.

Steady-state Kinetics and Inhibitory Action of Antitubercular Phenothiazines on Mycobacterium tuberculosis Type-II NADH-Menaquinone Oxidoreductase (NDH-2)*

H. Rubin, E. Weinstein, T. Yano, 2006, Journal of Biological Chemistry.

Ribonucleotide Reduction in Mycobacterium tuberculosis: Function and Expression of Genes Encoding Class Ib and Class II Ribonucleotide Reductases

G. Kaplan, Juliano Timm, J. Mckinney, 2003, Infection and Immunity.

The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice

Harvey Rubin, John L. Dahl, Clifton E. Barry, 2003, Proceedings of the National Academy of Sciences of the United States of America.

The Stringent Response of Mycobacterium tuberculosis Is Required for Long-Term Survival

V. Mizrahi, C. Barry, H. Rubin, 2000, Journal of bacteriology.

Why, when and how does the poly(A) tail shorten during mRNA translation?

H. Rubin, M. Halim, 1993, The International journal of biochemistry.

Characterization of A units released from the poly(A) tract of rabbit globin mRNA during protein synthesis: possible role of the released ATP in synthesizing protein.

H. Rubin, M. Halim, 1988, Comparative biochemistry and physiology. B, Comparative biochemistry.

Crystal Structure of the Caspase Activator Human Granzyme B, a Proteinase Highly Specific for an Asp-P1 Residue

R. Huber, W. Bode, R. Kiefersauer, 2000, Biological chemistry.

Specific detection of human and rabbit glucagon mRNA using a synthetic oligodeoxynucleotide.

H. Rubin, R. Tullis, R. Gutierrez, 1980, Biochemical and biophysical research communications.

Cloning, expression, purification and characterization of DNA topoisomerase I of Mycobacterium tuberculosis.

H. Rubin, G. Lu, F. Yang, 1996, Gene.

The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity.

R. Huber, W. Bode, S. Strobl, 1999, Journal of molecular biology.

Differential regulation of opposing RelMtb activities by the aminoacylation state of a tRNA.ribosome.mRNA.RelMtb complex.

H. Rubin, D Avarbock, A Avarbock, 2000, Biochemistry.

Inhibiting the stringent response blocks Mycobacterium tuberculosis entry into quiescence and reduces persistence

J. Bader, Gonzalo Colmenarejo, P. Karakousis, 2019, Science Advances.

Small Molecules Targeting Mycobacterium tuberculosis Type II NADH Dehydrogenase Exhibit Antimycobacterial Activity.

C. Vilchèze, W. Jacobs, H. M. Petrassi, 2018, Angewandte Chemie.

The Role of the Novel Exopolyphosphatase MT0516 in Mycobacterium tuberculosis Drug Tolerance and Persistence

P. Karakousis, N. Morrison, H. Rubin, 2011, PloS one.

Cloning, sequence determination, and regulation of the ribonucleotide reductase subunits from Plasmodium falciparum: a target for antimalarial therapy.

B. Cooperman, H. Rubin, Z. M. Wang, 1993, Proceedings of the National Academy of Sciences of the United States of America.

R2 C-terminal peptide inhibition of mammalian and yeast ribonucleotide reductase.

B. Cooperman, H. Rubin, A. Fisher, 1993, Journal of medicinal chemistry.

Functional regulation of the opposing (p)ppGpp synthetase/hydrolase activities of RelMtb from Mycobacterium tuberculosis.

H. Rubin, M. Buckstein, D. Avarbock, 2005, Biochemistry.

Comparative Trajectories of Active and S195A Inactive Trypsin upon Binding to Serpins*

L. Hedstrom, Y. Mély, N. Srividya, 2002, The Journal of Biological Chemistry.

Identification of residual structure within denatured antichymotrypsin: implications for serpin folding and misfolding.

Lisa D. Cabrita, S. Bottomley, M. Gore, 2004, Biochemical and biophysical research communications.

Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop

B. Cooperman, D. Christianson, H. Rubin, 1994, Nature Structural Biology.

Do pyrimidine nucleotides regulate translatability of globin mRNA as purine nucleotides do?

H. Rubin, M. Halim, E. Almendarez, 1988, The International journal of biochemistry.

The Kinetic Mechanism of Serpin-Proteinase Complex Formation

B. Cooperman, H. Rubin, K. O'Malley, 1997, The Journal of Biological Chemistry.

Conformational Change and Intermediates in the Unfolding of α1-Antichymotrypsin*

S. Bottomley, H. Rubin, M. Pearce, 2000, The Journal of Biological Chemistry.

Diverse Effects of pH on the Inhibition of Human Chymase by Serpins*

T. Selwood, M. Plotnick, H. Rubin, 1997, The Journal of Biological Chemistry.

Arginine substitutions in the hinge region of antichymotrypsin affect serpin β-sheet rearrangement

C. Lukacs, B. Cooperman, D. Christianson, 1996, Nature Structural Biology.

Crystallization, activity assay and preliminary X-ray diffraction analysis of the uncleaved form of the serpin antichymotrypsin.

B. Cooperman, D. Christianson, H. Rubin, 1992, Journal of molecular biology.

Type II NADH: menaquinone oxidoreductase of Mycobacterium tuberculosis.

H. Rubin, T. Yano, J. Teh, 2007, Infectious disorders drug targets.

Mycobacterium tuberculosis Type II NADH-Menaquinone Oxidoreductase Catalyzes Electron Transfer through a Two-Site Ping-Pong Mechanism and Has Two Quinone-Binding Sites

H. Rubin, N. Schechter, T. Yano, 2014, Biochemistry.

Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis.

H. Rubin, Z. M. Wang, D Avarbock, 1999, Gene.

Acinetobacter baumannii OxPhos inhibitors as selective anti-infective agents.

K. Freeman, T. Selwood, R. Scott, 2015, Bioorganic & Medicinal Chemistry Letters.

Physician's Guide to Terrorist Attack

H. Rubin, 2004, Annals of Internal Medicine.

Investigating metabolite essentiality through genome scale analysis of E . coli production capabilities

Harvey Rubin, Á. Halász, H. Rubin, 2004 .

Conformational statistics of short RNA chains

N. Kallenbach, H. Rubin, 1975 .

The Stable Tyrosyl Radical in Mouse Ribonucleotide Reductase Is Not Essential for Enzymic Activity

B. Cooperman, H. Rubin, J. Salem, 1994 .

Characterization of mRNA Interferases from Mycobacterium tuberculosis*

M. Inouye, Ling Zhu, N. Connell, 2006, Journal of Biological Chemistry.

Looking for the DNA killer app

Harvey Rubin, H. Rubin, 1996, Nature Structural Biology.