J. Salerno

发表

Novel cell-penetrating peptide-adaptors effect intracellular delivery and endosomal escape of protein cargos

Jonathan L. McMurry, J. McMurry, S. J. Nowak, 2016, Journal of Cell Science.

MAP kinases bind endothelial nitric oxide synthase

Jonathan L. McMurry, J. McMurry, J. Salerno, 2012, FEBS open bio.

Steroidogenic electron transport in adrenal cortex mitochondria

J. Lancaster, J. Lambeth, H. Kamin, 1982, Molecular and Cellular Biochemistry.

NADPH analog binding to constitutive nitric oxide activates electron transfer and NO synthesis.

J. Salerno, Rachel J. Jones, Y. Gao, 2006, Nitric oxide.

Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs

D. Spratt, J. G. Guillemette, J. Salerno, 2006, The FEBS journal.

Identification and characterization of VPO1, a new animal heme-containing peroxidase.

J. Lambeth, G. Cheng, P. Pagano, 2008, Free radical biology & medicine.

Titration of Low Kd Binding Sites: Binding of Arginine Analogs to Nitric Oxide Synthases

P. Martásek, L. Roman, J. Salerno, 2001 .

Thermodynamic and EPR characteristics of two ferredoxin-type iron-sulfur centers in the succinate-ubiquinone reductase segment of the respiratory chain.

T. Ohnishi, J. Salerno, 1976, The Journal of biological chemistry.

Determination of the exchange integral in binuclear iron-sulfur clusters in proteins of varying complexity.

J. Leigh, T. Ohnishi, J. Salerno, 1977, Biochimica et biophysica acta.

GTP Cyclohydrolase I Phosphorylation and Interaction With GTP Cyclohydrolase Feedback Regulatory Protein Provide Novel Regulation of Endothelial Tetrahydrobiopterin and Nitric Oxide

D. Harrison, H. Jo, A. Husain, 2010, Circulation research.

iNOS regulation by calcium/calmodulin-dependent protein kinase II in vascular smooth muscle.

H. Singer, J. Salerno, D. Jourd’heuil, 2007, American journal of physiology. Heart and circulatory physiology.

A dibenz[a,c]phenazine-supported N-heterocyclic carbene and its rhodium and iridium complexes

J. Salerno, D. Vanderveer, D. Tapu, 2014 .

The orientation of iron-sulfur clusters and a spin-coupled ubiquinone pair in the mitochondrial membrane.

T. Ohnishi, J. Salerno, H. Blum, 1979, Biochimica et biophysica acta.

Crystal field of atypical low-spin ferriheme complexes

J. Leigh, J. Salerno, 1984 .

Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase.

J. Salerno, 1984, The Journal of biological chemistry.

Exchange integral for a variety of tetranuclear ferredoxins.

P. Rich, T. Ohnishi, J. Salerno, 1979, Biochimica et biophysica acta.

The nature of the nitric oxide complexes of lipoxygenase.

J. Siedow, J. Salerno, 1979, Biochimica et biophysica acta.

EXCHANGE INTERACTION IN SPINACH FERREDOXIN DETERMINED BY ELECTRON PARAMAGNETIC RESONANCE1

J. Leigh, T. Ohnishi, J. Salerno, 1978 .

Electron paramagnetic resonance determination of a low-lying excited state in Chromatium vinosum high-potential iron protein.

J. Leigh, R. Prince, T. Ohnishi, 1977, Biophysical journal.

Structural analysis of the Trichodesmium nitrogenase iron protein: implications for aerobic nitrogen fixation activity.

J. Zehr, J. Salerno, D. Harris, 1997, FEMS microbiology letters.

Energy coupling in Mn2+ oxidation by a marine bacterium

Henry L. Ehrich, J. Salerno, 1990, Archives of Microbiology.

Modular structure of neuronal nitric oxide synthase: localization of the arginine binding site and modulation by pterin.

P. Martásek, Q. Liu, K. McMillan, 1995, Biochemical and biophysical research communications.

Five decades of research on mitochondrial NADH-quinone oxidoreductase (complex I)

S. Ohnishi, T. Ohnishi, J. Salerno, 2018, Biological chemistry.

Advances in Membrane Biochemistry and Bioenergetics

H. Tedeschi, J. Salerno, Chong-Ho Kim, 1988 .

Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment.

B. Matthews, I. Korndörfer, J. Salerno, 2000, Acta crystallographica. Section D, Biological crystallography.

Endonuclease III is an iron-sulfur protein.

R. Cunningham, H. Asahara, J. Bank, 1989, Biochemistry.

MAP kinases differentially bind and phosphorylate NOS3 via two unique NOS3 sites

J. McMurry, J. Salerno, C. Chrestensen, 2022, FEBS open bio.

Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo.

T. Ohnishi, J. Salerno, W. Ingledew, 1995, European journal of biochemistry.

Electron nuclear double resonance (ENDOR) of the Qc.- ubisemiquinone radical in the mitochondrial electron transport chain.

C. Scholes, M. Osgood, J. Salerno, 1990, Biochemistry.

Characterization by Electron Paramagnetic Resonance of the Interactions of L-Arginine and L-Thiocitrulline with the Heme Cofactor Region of Nitric Oxide Synthase (*)

R. F. Williams, B. Masters, K. McMillan, 1995, The Journal of Biological Chemistry.

A mathematical model of endothelial nitric oxide synthase activation with time delay exhibiting Hopf bifurcation and oscillations.

L. Ritter, J. Salerno, C. Chrestensen, 2016, Mathematical biosciences.

Studies on the stabilized ubisemiquinone species in the succinate-cytochrome c reductase segment of the intact mitochondrial membrane system.

T. Ohnishi, J. Salerno, 1980, The Biochemical journal.

The electron paramagnetic resonance spectra of partially purified cytochrome b 6 f complex from spinach

J. Salerno, G. Gerstle, J. McGill, 1983 .

Tetranuclear and binuclear iron-sulfur clusters in succinate dehydrogenase: a method of iron quantitation by formation of paramagnetic complexes.

T. Ohnishi, J. Salerno, 1976, Biochemical and biophysical research communications.

Magnetic interactions in milk xanthine oxidase.

J. Salerno, M. Barber, L. Siegel, 1982, Biochemistry.

2 – Nitric Oxide Complexes of Metalloproteins: An Introductory Overview

J. Salerno, 1996 .

Angular dependences of perpendicular and parallel mode electron paramagnetic resonance of oxidized beef heart cytochrome c oxidase.

A. Thomson, V. Oganesyan, J. Salerno, 2000, Biophysical journal.

Exchange coupling between siroheme and iron-sulfur ([4Fe-4S]) cluster in E. coli sulfite reductase. Moessbauer studies and coupling models for a 2-electron reduced enzyme state and complexes with sulfide

J. Salerno, J. Christner, P. A. Janick, 1984 .

Exchange coupling in spinach ferredoxin determined by resonance Raman spectroscopy.

J. Leigh, F. Adar, J. Salerno, 1977, Biochemical and biophysical research communications.

Inhibition of nitric oxide synthase by cobalamins and cobinamides.

N. Jiang, J. Weinberg, J. Salerno, 2009, Free radical biology & medicine.

A model for the simulation of the EPR spectra of chromophores in partially oriented membrane multilayers

J. Leigh, J. Salerno, H. Blum, 1978 .

The orientation of bovine adrenal cortex cytochrome P-450 in submitochondrial particle multilayers.

J. Leigh, T. Ohnishi, J. Salerno, 1978, Archives of biochemistry and biophysics.

The orientation of a heme of cytochrome c oxidase in submitochondrial particles.

B. Chance, J. Leigh, H. Harmon, 1978, Biochimica et biophysica acta.

Strong-field and integral spin-ligand complexes of the cytochrome bo quinol oxidase in Escherichia coli membrane preparations.

R. Gennis, J. Salerno, W. Ingledew, 1994, Biochimica et biophysica acta.

MnO2 Reduction by Marine Mn2+ Oxidizing Bacteria from Around Hydrothermal Vents at a Mid-Ocean Spreading Center and from the Black Sea

L. Graham, J. Salerno, H. Ehrlich, 1991 .

Effects of ethanol and acetaldehyde on iron-sulfur centers in the mitochondrial respiratory chain

T. Ohnishi, J. Salerno, 1976 .

Studies on electron paramagnetic resonance spectra manifested by a respiratory chain hydrogen carrier.

T. Ohnishi, J. Salerno, W. Ingledew, 1976, Archives of biochemistry and biophysics.

Nitric oxide synthases: domain structure and alignment in enzyme function and control.

J. Salerno, D. Ghosh, 2003, Frontiers in bioscience : a journal and virtual library.

Theoretical and Practical Aspects of Studying Molybdenum-containing Enzymes

J. Salerno, M. Barber, 1980 .

The role of the conserved COOH-terminal triad in alphaA-crystallin aggregation and functionality.

J. Koretz, Ying-Lan Li, K. R. Schmitz, 2005, Molecular vision.

Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region.

J. Koretz, C. Eifert, J. Salerno, 2003, Protein engineering.

INSULT: a novel mutagenesis method generating high yields of closed circular mutant DNA with one primer per mutant.

J. Salerno, Rachel J. Jones, Susan M E Smith, 2005, Molecular biotechnology.

Potentiometric titration of cytochrome‐bo type quinol oxidase of Escherichia coli: Evidence for heme‐heme and copper‐heme interaction

J. Salerno, W. Ingledew, B. Bolgiano, 1989, FEBS letters.

The spatial relationships and structure of the binuclear iron-sulfur clusters in succinate dehydrogenase.

T. Ohnishi, J. Salerno, T. King, 1979, The Journal of biological chemistry.

Electron Transport in The Cytochrome B6F Complex

J. Salerno, J. W. McGill, 1987 .

Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli.

R. Gennis, R. Poole, J. Salerno, 1990, The Journal of biological chemistry.

Ligand binding to the haem-copper binuclear catalytic site of cytochrome bo, a respiratory quinol oxidase from Escherichia coli.

J. Salerno, W. D. Horrocks, W. Ingledew, 1993, European journal of biochemistry.

Spatial relationship between cytochrome a and a3.

T. Ohnishi, J. Salerno, T. Frey, 1982, The Journal of biological chemistry.

Stabilized ubisemiquinone in reconstituted succinate ubiquinone reductase.

Y. Wei, J. Salerno, T. King, 1987, Biochemical and biophysical research communications.

The Role of a Conserved Serine Residue within Hydrogen Bonding Distance of FAD in Redox Properties and the Modulation of Catalysis by Ca2+/Calmodulin of Constitutive Nitric-oxide Synthases*

B. Masters, P. Martásek, L. Roman, 2006, Journal of Biological Chemistry.

Thermodynamics of Oxidation-Reduction Reactions in Mammalian Nitric-oxide Synthase Isoforms*

P. Martásek, L. Roman, J. G. Guillemette, 2004, Journal of Biological Chemistry.

Substrate and substrate analog binding to endothelial nitric oxide synthase: electron paramagnetic resonance as an isoform-specific probe of the binding mode of substrate analogs.

R. F. Williams, B. Masters, P. Martásek, 1997, Biochemistry.

Nitric Oxide Synthases: Structure, Function, and Control

J. Salerno, Susan M E Smith, Ch. E. L. Brown, 1998 .

Molecular modeling of the 3-D structure of cytochrome P-450scc.

J. Salerno, S. Vijayakumar, 1992, Biochimica et biophysica acta.

An Autoinhibitory Control Element Defines Calcium-regulated Isoforms of Nitric Oxide Synthase*

B. Masters, P. Martásek, L. Roman, 1997, The Journal of Biological Chemistry.

A spin 3/2 ferrous—nitric oxide derivative of an iron‐containing moiety associated with Neurospora crassa and higher plant mitochondria

P. Rich, J. Salerno, J. Leigh, 1978 .

Kinetic and Spectroscopic Studies of Bicupin Oxalate Oxidase and Putative Active Site Mutants

A. Ozarowski, E. W. Moomaw, A. Angerhofer, 2013, PloS one.

7 – Ubisemiquinones in Electron-Transfer Systems of Mitochondria

T. Ohnishi, J. Salerno, H. Blum, 1982 .

A transmembrane quinone pair in the succinate dehydrogenase‐cytochrome b region

T. Ohnishi, H. J. Harmon, J. Salerno, 1977, FEBS letters.

Electron Transfer Components of Manganese Oxidizing Bacteria

L. Graham, J. Salerno, H. Ehrlich, 1987 .

Purification and characterization of low potential c cytochromes from Desulfovibrio desulfuricans membranes

D. Pope, J. Salerno, J. Kramer, 1986 .

Conformation‐driven and semiquinone‐gated proton‐pump mechanism in the NADH‐ubiquinone oxidoreductase (complex I)

Tomoko Ohnishi, T. Ohnishi, J. Salerno, 2005, FEBS letters.

Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli.

R. Gennis, J. Salerno, W. Ingledew, 1998, European journal of biochemistry.

Spin coupling between electron carriers in the dehydrogenase segments of the respiratory chain.

T. Ohnishi, J. Salerno, 1977, Biochemical and biophysical research communications.

The C331A Mutant of Neuronal Nitric-Oxide Synthase Is Defective in Arginine Binding*

R. T. Miller, B. Masters, M. Ikeda-Saito, 1998, The Journal of Biological Chemistry.

Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I).

S. Ohnishi, T. Ohnishi, J. Salerno, 2010, Biochimica et biophysica acta.

Novel cell-penetrating peptide-adaptors effect intracellular delivery and endosomal escape of protein cargos

J. McMurry, J. Salerno, C. Chrestensen, 2016, Journal of Cell Science.

Erratum for "Inhibition of Nitric Oxide Synthase by Cobalamins and Cobinamides," [Free Radic. Biol. Med. 46:1626–1632, 2009]

N. Jiang, J. Salerno, D. Ghosh, 2011 .

Differential Activation of Nitric-oxide Synthase Isozymes by Calmodulin-Troponin C Chimeras*

D. Spratt, J. G. Guillemette, J. Salerno, 2004, Journal of Biological Chemistry.

Calmodulin activates neuronal nitric oxide synthase by enabling transitions between conformational states

T. Poulos, Huiying Li, K. Ray, 2013, FEBS letters.

FMN fluorescence in inducible NOS constructs reveals a series of conformational states involved in the reductase catalytic cycle

K. Ray, J. Salerno, D. Ghosh, 2012, The FEBS journal.

Direct measurement by laser flash photolysis of intraprotein electron transfer in a rat neuronal nitric oxide synthase.

G. Tollin, Changjian Feng, J. G. Guillemette, 2007, Journal of the American Chemical Society.

Intraprotein electron transfer in a two-domain construct of neuronal nitric oxide synthase: the output state in nitric oxide formation.

G. Tollin, Changjian Feng, J. Salerno, 2006, Biochemistry.

Nitric oxide synthases: analogies to cytochrome P450 monooxygenases and characterization of recombinant rat neuronal nitric oxide synthase hemoprotein.

B. Masters, K. McMillan, J. Salerno, 1996, Methods in enzymology.

Ligand, cofactor, and residue vibrations in the catalytic site of endothelial nitric oxide synthase.

P. Rich, J. Salerno, W. Ingledew, 2005, Biochemistry.

Neuronal nitric oxide synthase ligand and protein vibrations at the substrate binding site. A study by FTIR.

P. Rich, J. Salerno, W. Ingledew, 2002, Biochemistry.

Angular dependence of electron paramagnetic resonances of an azide-NO complex of cytochrome c oxidase: orientation of the haem-copper axis in cytochrome aa3 from ox heart.

J. Salerno, W. Ingledew, D. J. Hunter, 1998, Biochimica et biophysica acta.

The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a ‘g = 12’ EPR feature analogous to that of ‘slow’ cytochrome oxidase

R. Gennis, J. Salerno, M. Calhoun, 1992, FEBS letters.

Aspects of Spin Coupling Between Even and Odd Electron Systems: Applications To Succinate: Q Reductase

J. Salerno, Xu Yan, 1987 .

Binding of intermediate, product, and substrate analogs to neuronal nitric oxide synthase: ferriheme is sensitive to ligand-specific effects in the L-arginine binding site.

B. Masters, K. McMillan, J. Salerno, 1996, Biochemistry.

Substrate binding-induced changes in the EPR spectra of the ferrous nitric oxide complexes of neuronal nitric oxide synthase

M. Ikeda-Saito, P. Martásek, C. T. Migita, 1997 .

Pathways of Electron Transfer in Desulfovibrio

D. Pope, J. Salerno, J. Kramer, 1987 .

Space, time and nitric oxide – neuronal nitric oxide synthase generates signal pulses

J. Salerno, John C Salerno, D. Ghosh, 2009, The FEBS journal.

Neuronal nitric oxide synthase: Prototype for pulsed enzymology

J. Salerno, 2008, FEBS letters.

Nitric-oxide Synthase Output State

J. Salerno, D. Ghosh, J. Weinberg, 2006, Journal of Biological Chemistry.

Control of eNOS and nNOS through regulation of obligatory conformational changes in the reductase catalytic cycle

Jonathan L. McMurry, Israel M. Scott, J. McMurry, 2018, bioRxiv.

The Function of the Small Insertion in the Hinge Subdomain in the Control of Constitutive Mammalian Nitric-oxide Synthases*

Kevin J Mann, J. Salerno, Bradley S. DeMay, 2004, Journal of Biological Chemistry.

Endothelial nitric oxide synthase is regulated by ERK phosphorylation at Ser602

Jonathan L. McMurry, J. McMurry, R. Razdan, 2014, Bioscience reports.

The EPR spectra of the cytochrome b-c1 complex of Rhodopseudomonas sphaeroides.

L. Yu, J. Salerno, M. Doyle, 1986, Biochemical and biophysical research communications.

N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function.

J. Koretz, C. Eifert, J. Salerno, 2005, Biochimica et Biophysica Acta.

Electron-paramagnetic-resonance lineshapes of biological molecules: some effects of distributed parameters.

J. Salerno, 1985, Biochemical Society transactions.

Rate, affinity and calcium dependence of nitric oxide synthase isoform binding to the primary physiological regulator calmodulin

Jonathan L. McMurry, Israel M. Scott, J. McMurry, 2011, The FEBS journal.

Thermodynamic and spectroscopic characteristics of the cytochrome bc1 complex. Role of quinone in the behavior of cytochrome b562.

M. Osgood, J. Salerno, T. King, 1989, The Journal of biological chemistry.

Understanding the structural aspects of neuronal nitric oxide synthase (NOS) using microdissection by molecular cloning techniques: molecular dissection of neuronal NOS.

B. Masters, E. Sheta, P. Martásek, 1996, Advances in experimental medicine and biology.

An Autoinhibitory Control Element Defines Calcium-regulated Isoforms of Nitric Oxide Synthase*

B. Masters, P. Martásek, L. Roman, 1997, The Journal of Biological Chemistry.

Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase.

J. Bowyer, T. Ohnishi, J. Salerno, 1981, The Journal of biological chemistry.

Thermodynamic resolution of cytochrome P450 and characterization of an iron-sulfur center in rat liver microsomal preparations.

T. Ohnishi, J. Salerno, W. Ingledew, 1976, Archives of biochemistry and biophysics.

Anti‐ferromagnetic exchange in beef adrenodoxin as measured by resonance raman spectroscopy

F. Adar, T. Ohnishi, J. Salerno, 1977, FEBS letters.