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Article ; Online: Letter by Stamler et al Regarding Article, "Nitrite and

Stamler, Jonathan S / Reynolds, James D / Hess, Douglas T

2017 Volume 135, Issue 24, Page(s) e1135–e1136

MeSH term(s)	Exercise ; Hemoglobins ; Humans ; Hypoxia ; Nitrites
Chemical Substances	Hemoglobins ; Nitrites ; S-nitrosohemoglobin
Language	English
Publishing date	2017-06-09
Publishing country	United States
Document type	Letter ; Comment
ZDB-ID	80099-5
ISSN	1524-4539 ; 0009-7322 ; 0069-4193 ; 0065-8499
ISSN (online)	1524-4539
ISSN	0009-7322 ; 0069-4193 ; 0065-8499
DOI	10.1161/CIRCULATIONAHA.117.027071
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Article ; Online: S-nitrosylation is required for β

Fonseca, Fabio V / Raffay, Thomas M / Xiao, Kunhong / McLaughlin, Precious J / Qian, Zhaoxia / Grimmett, Zachary W / Adachi, Naoko / Wang, Benlian / Hausladen, Alfred / Cobb, Brian A / Zhang, Rongli / Hess, Douglas T / Gaston, Benjamin / Lambert, Nevin A / Reynolds, James D / Premont, Richard T / Stamler, Jonathan S

Molecular cell

2022 Volume 82, Issue 16, Page(s) 3089–3102.e7

Abstract: ... The ... ...

Abstract	The β
MeSH term(s)	Animals ; Asthma/chemically induced ; Asthma/genetics ; Mice ; Signal Transduction
Language	English
Publishing date	2022-08-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.06.033
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Article ; Online: Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling.

Stomberski, Colin T / Hess, Douglas T / Stamler, Jonathan S

Antioxidants & redox signaling

2018 Volume 30, Issue 10, Page(s) 1331–1351

Abstract: Significance: Protein S-nitrosylation, the oxidative modification of cysteine by nitric oxide (NO) to form protein S-nitrosothiols (SNOs), mediates redox-based signaling that conveys, in large part, the ubiquitous influence of NO on cellular function. S- ...

Abstract	Significance: Protein S-nitrosylation, the oxidative modification of cysteine by nitric oxide (NO) to form protein S-nitrosothiols (SNOs), mediates redox-based signaling that conveys, in large part, the ubiquitous influence of NO on cellular function. S-nitrosylation regulates protein activity, stability, localization, and protein-protein interactions across myriad physiological processes, and aberrant S-nitrosylation is associated with diverse pathophysiologies. Recent Advances: It is recently recognized that S-nitrosylation endows S-nitroso-protein (SNO-proteins) with S-nitrosylase activity, that is, the potential to trans-S-nitrosylate additional proteins, thereby propagating SNO-based signals, analogous to kinase-mediated signaling cascades. In addition, it is increasingly appreciated that cellular S-nitrosylation is governed by dynamically coupled equilibria between SNO-proteins and low-molecular-weight SNOs, which are controlled by a growing set of enzymatic denitrosylases comprising two main classes (high and low molecular weight). S-nitrosylases and denitrosylases, which together control steady-state SNO levels, may be identified with distinct physiology and pathophysiology ranging from cardiovascular and respiratory disorders to neurodegeneration and cancer. Critical issues: The target specificity of protein S-nitrosylation and the stability and reactivity of protein SNOs are determined substantially by enzymatic machinery comprising highly conserved transnitrosylases and denitrosylases. Understanding the differential functionality of SNO-regulatory enzymes is essential, and is amenable to genetic and pharmacological analyses, read out as perturbation of specific equilibria within the SNO circuitry. Future directions: The emerging picture of NO biology entails equilibria among potentially thousands of different SNOs, governed by denitrosylases and nitrosylases. Thus, to elucidate the operation and consequences of S-nitrosylation in cellular contexts, studies should consider the roles of SNO-proteins as both targets and transducers of S-nitrosylation, functioning according to enzymatically governed equilibria.
MeSH term(s)	Animals ; Cysteine/metabolism ; Humans ; Nitric Oxide/metabolism ; Oxidation-Reduction ; Proteins/metabolism ; S-Nitrosothiols/metabolism ; Signal Transduction
Chemical Substances	Proteins ; S-Nitrosothiols ; Nitric Oxide (31C4KY9ESH) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2018-01-10
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2017.7403
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Article ; Online: Editorial for "Methods for analysis of nitric oxide signalling by S-nitrosylation".

Hess, Douglas T / Stamler, Jonathan S

Methods (San Diego, Calif.)

2013 Volume 62, Issue 2, Page(s) 121–122

MeSH term(s)	Animals ; Humans ; Nitric Oxide/physiology ; Protein Processing, Post-Translational ; S-Nitrosothiols/metabolism ; Signal Transduction
Chemical Substances	S-Nitrosothiols ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2013-08-01
Publishing country	United States
Document type	Editorial
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2013.08.009
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Article ; Online: Dosing Matters! Vitamin C in Critical Illness.

Long, Micah T / Hess, Aaron S / Ries, Michael P / Coursin, Douglas B

Critical care medicine

2019 Volume 47, Issue 12, Page(s) e1042

MeSH term(s)	Ascorbic Acid ; Critical Illness ; Humans ; Randomized Controlled Trials as Topic ; Vitamin D ; Vitamin D Deficiency
Chemical Substances	Vitamin D (1406-16-2) ; Ascorbic Acid (PQ6CK8PD0R)
Language	English
Publishing date	2019-11-18
Publishing country	United States
Document type	Letter ; Comment
ZDB-ID	197890-1
ISSN	1530-0293 ; 0090-3493
ISSN (online)	1530-0293
ISSN	0090-3493
DOI	10.1097/CCM.0000000000004006
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Article ; Online: Differential

Adachi, Naoko / Hess, Douglas T / Kaku, Mika / Ueda, Chie / Numa, Chisato / Saito, Naoaki

The Journal of biological chemistry

2018 Volume 294, Issue 7, Page(s) 2569–2578

Abstract: With few reported exceptions, G protein-coupled receptors (GPCRs) are modified by Cys palmitoylation ( ...

Abstract	With few reported exceptions, G protein-coupled receptors (GPCRs) are modified by Cys palmitoylation (
MeSH term(s)	Amino Acid Substitution ; Animals ; HEK293 Cells ; Humans ; Lipoylation ; Mice ; Mutation, Missense ; Protein Structure, Secondary ; Receptors, Adrenergic, beta-3/genetics ; Receptors, Adrenergic, beta-3/metabolism ; Species Specificity
Chemical Substances	Receptors, Adrenergic, beta-3
Language	English
Publishing date	2018-12-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.004978
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Article ; Online: Use of adhesive cranial bone flap fixation without hardware to improve mechanical strength, resist cerebrospinal fluid leakage, and maintain anatomical alignment: a laboratory study.

Smith, Timothy R / Foley, Kevin T / Boruah, Sourabh / Slotkin, Jonathan R / Woodard, Eric / Lazor, John B / Cavaleri, Christy / Brown, Michael C / McDonough, Brittany / Hess, Brian / Van Citters, Douglas W

Journal of neurosurgery

2022 , Page(s) 1–11

Abstract: Objective: Titanium plates and screws (TPS) are the current standard of care for fixation of cranial bone flaps. These materials have been used for decades but have known potential complications, including flap migration, bone resorption/incomplete ... ...

Abstract	Objective: Titanium plates and screws (TPS) are the current standard of care for fixation of cranial bone flaps. These materials have been used for decades but have known potential complications, including flap migration, bone resorption/incomplete osseous union, hardware protrusion, cosmetic deformity, wound infection/dehiscence, and cerebrospinal fluid (CSF) leakage. This study evaluated the efficacy of a novel mineral-organic bone adhesive (Tetranite) for cranial bone flap fixation. Methods: Craniotomy bone flaps created in human cadaveric skulls were tested under quasistatic and impact loading in the following conditions: 1) uncut skull; 2) bone flaps fixated with TPS alone; and 3) bone flaps fixated with bone adhesive alone. All fixative surgical procedures were performed by a group of 16 neurosurgeons in a simulated surgical environment. The position of adhesive-fixated cranial bone flaps was measured using computed tomography and compared with their original native location. The resistance of adhesive-fixated cranial bone flaps to simulated CSF leakage was also evaluated. Because there was a gap around the circumference of the TPS-fixated specimens that was visible to the naked eye, pressurized CSF leak testing was not attempted on them. Results: Adhesive-fixated bone flaps showed significantly stiffer and stronger quasistatic responses than TPS-fixated specimens. The strength and stiffness of the adhesive-fixated specimens were not significantly different from those of the uncut native skulls. Total and plastic deflections under 6-J impact were significantly less for adhesive-fixed bone flaps than TPS. There were no significant differences in any subthreshold impact metrics between the adhesive-fixed and native specimens at both 6-J and 12-J impact levels, with 1 exception. Plastic deflection at 6-J impact was significantly less in adhesive-fixated bone flaps than in native specimens. The energy to failure of the adhesive-fixated specimens was not significantly different from that of the native specimens. Time since fixation (20 minutes vs 10 days) did not significantly affect the impact failure properties of the adhesive-fixated specimens. Of the 16 adhesive-fixated craniotomy specimens tested, 14 did not leak at pressures as high as 40 mm Hg. Conclusions: The neurosurgeons in this study had no prior exposure or experience with the bone adhesive. Despite this, improved resistance to CSF egress, superior mechanical properties, and better cosmetic outcomes were demonstrated with bone adhesive compared with TPS.
Language	English
Publishing date	2022-12-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	3089-2
ISSN	1933-0693 ; 0022-3085
ISSN (online)	1933-0693
ISSN	0022-3085
DOI	10.3171/2022.10.JNS221657
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Article ; Online: Regulation by S-nitrosylation of protein post-translational modification.

Hess, Douglas T / Stamler, Jonathan S

The Journal of biological chemistry

2011 Volume 287, Issue 7, Page(s) 4411–4418

Abstract: Protein post-translational modification by S-nitrosylation conveys a ubiquitous influence of nitric oxide on signal transduction in eukaryotic cells. The wide functional purview of S-nitrosylation reflects in part the regulation by S-nitrosylation of the ...

Abstract	Protein post-translational modification by S-nitrosylation conveys a ubiquitous influence of nitric oxide on signal transduction in eukaryotic cells. The wide functional purview of S-nitrosylation reflects in part the regulation by S-nitrosylation of the principal protein post-translational modifications that play a role in cell signaling, including phosphorylation, acetylation, ubiquitylation and related modifications, palmitoylation, and alternative Cys-based redox modifications. In this minireview, we discuss the mechanisms through which S-nitrosylation exerts its broad pleiotropic influence on protein post-translational modification.
MeSH term(s)	Acetylation ; Animals ; Humans ; Nitric Oxide/metabolism ; Phosphorylation/physiology ; Protein Processing, Post-Translational/physiology ; Signal Transduction/physiology
Chemical Substances	Nitric Oxide (31C4KY9ESH)
Keywords	covid19
Language	English
Publishing date	2011-12-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.R111.285742
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Article ; Online: A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation.

Seth, Divya / Hess, Douglas T / Hausladen, Alfred / Wang, Liwen / Wang, Ya-Juan / Stamler, Jonathan S

Molecular cell

2018 Volume 69, Issue 3, Page(s) 451–464.e6

Abstract: S-nitrosylation, the oxidative modification of Cys residues by nitric oxide (NO) to form S-nitrosothiols (SNOs), modifies all main classes of proteins and provides a fundamental redox-based cellular signaling mechanism. However, in contrast to other post- ...

Abstract	S-nitrosylation, the oxidative modification of Cys residues by nitric oxide (NO) to form S-nitrosothiols (SNOs), modifies all main classes of proteins and provides a fundamental redox-based cellular signaling mechanism. However, in contrast to other post-translational protein modifications, S-nitrosylation is generally considered to be non-enzymatic, involving multiple chemical routes. We report here that endogenous protein S-nitrosylation in the model organism E. coli depends principally upon the enzymatic activity of the hybrid cluster protein Hcp, employing NO produced by nitrate reductase. Anaerobiosis on nitrate induces both Hcp and nitrate reductase, thereby resulting in the S-nitrosylation-dependent assembly of a large interactome including enzymes that generate NO (NO synthase), synthesize SNO-proteins (SNO synthase), and propagate SNO-based signaling (trans-nitrosylases) to regulate cell motility and metabolism. Thus, protein S-nitrosylation by NO in E. coli is essentially enzymatic, and the potential generality of the multiplex enzymatic mechanism that we describe may support a re-conceptualization of NO-based cellular signaling.
MeSH term(s)	Cysteine/metabolism ; Escherichia coli ; Escherichia coli Proteins ; Nitric Oxide/metabolism ; Nitrosation/physiology ; Oxidation-Reduction ; Protein Processing, Post-Translational/physiology ; Proteins/metabolism ; Proteolysis ; Proteomics/methods ; S-Nitrosothiols/metabolism ; Signal Transduction
Chemical Substances	Escherichia coli Proteins ; Proteins ; S-Nitrosothiols ; Nitric Oxide (31C4KY9ESH) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2018-01-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2017.12.025
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Article ; Online: Identifying single S-nitrosothiol sites with cardioprotection.

Anand, Puneet / Hess, Douglas T / Stamler, Jonathan S

Circulation research

2013 Volume 113, Issue 7, Page(s) 849–851

MeSH term(s)	Animals ; Cysteine/metabolism ; Electron Transport Complex I/metabolism ; Male ; Mitochondria, Heart/metabolism ; Mitochondrial Proteins/metabolism ; Myocardial Reperfusion Injury/prevention & control
Chemical Substances	Mitochondrial Proteins ; Electron Transport Complex I (EC 1.6.5.3) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2013-09-13
Publishing country	United States
Document type	Comment ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.113.302332
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