Theory and modelling of diamond fracture from an atomic perspective

Brenner, Donald W.; Shenderova, Olga

doi:10.1098/rsta.2014.0139

Cited by 11 publications

(8 citation statements)

References 41 publications

(71 reference statements)

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“…TNF-dependent phosphorylation relies on the correct localization of kinases and their substrates and requires subcellular protein translocation 33 . TNF binding to its receptor recruits a range of complex members to the plasma membrane and binding of TRAF2, and requirement of TRADD, RIPK1, IAPs, and the LUBAC complex for proper activation of TAK1 is well documented 34 . However, the impact of phosphorylation on protein localization is less explored.…”

Section: Resultsmentioning

confidence: 99%

Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling

et al. 2021

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Tumor necrosis factor (TNF) is one of the few cytokines successfully targeted by therapies against inflammatory diseases. However, blocking this well studied and pleiotropic ligand can cause dramatic side-effects. Here, we reason that a systems-level proteomic analysis of TNF signaling could dissect its diverse functions and offer a base for developing more targeted therapies. Therefore, we combine phosphoproteomics time course experiments with subcellular localization and kinase inhibitor analysis to identify functional modules of protein phosphorylation. The majority of regulated phosphorylation events can be assigned to an upstream kinase by inhibiting master kinases. Spatial proteomics reveals phosphorylation-dependent translocations of hundreds of proteins upon TNF stimulation. Phosphoproteome analysis of TNF-induced apoptosis and necroptosis uncovers a key role for transcriptional cyclin-dependent kinase activity to promote cytokine production and prevent excessive cell death downstream of the TNF signaling receptor. This resource of TNF-induced pathways and sites can be explored at http://tnfviewer.biochem.mpg.de/.

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Section: Resultsmentioning

confidence: 99%

Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling

et al. 2021

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“…Upon B-doping, B−B and B−C clusters are formed within the diamond grains, 65 which exhibit weaker bonding energies compared to the strong hybrid sp 3 C−C bonds, 66 and result in local expansion of the diamond crystal lattice. 67 The incorporated B−B and B−C clusters will thus act as "weak" spots of the lattice, whereby the amorphization is locally enhanced or even initialized during sliding.…”

Section: Methodsmentioning

confidence: 99%

Effect of Boron Doping on the Wear Behavior of the Growth and Nucleation Surfaces of Micro- and Nanocrystalline Diamond Films

Buijnsters

Tsigkourakos

Hantschel

et al. 2016

ACS Appl. Mater. Interfaces

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Effect of boron doping on the wear behavior of the growth and nucleation surfaces of micro-and nanocrystalline diamond films Buijnsters CopyrightOther than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons. Takedown policyPlease contact us and provide details if you believe this document breaches copyrights. We will remove access to the work immediately and investigate your claim. ABSTRACT: B-doped diamond has become the ultimate material for applications in the field of microelectromechanical systems (MEMS), which require both highly wear resistant and electrically conductive diamond films and microstructures. Despite the extensive research of the tribological properties of undoped diamond, to date there is very limited knowledge of the wear properties of highly B-doped diamond. Therefore, in this work a comprehensive investigation of the wear behavior of highly B-doped diamond is presented. Reciprocating sliding tests are performed on micro-and nanocrystalline diamond (MCD, NCD) films with varying B-doping levels and thicknesses. We demonstrate a linear dependency of the wear rate of the different diamond films with the B-doping level. Specifically, the wear rate increases by a factor of 3 between NCD films with 0.6 and 2.8 at. % B-doping levels. This increase in the wear rate can be linked to a 50% decrease in both hardness and elastic modulus of the highly B-doped NCD films, as determined by nanoindentation measurements. Moreover, we show that fine-grained diamond films are more prone to wear. Particularly, NCD films with a 3× smaller grain size but similar B-doping levels exhibit a double wear rate, indicating the crucial role of the grain size on the diamond film wear behavior. On the other hand, MCD films are the most wear-resistant films due to their larger grains and lower B-doping levels. We propose a graphical scheme of the wear behavior which involves planarization and mechanochemically driven amorphization of the surface to describe the wear mechanism of B-doped diamond films. Finally, the wear behavior of the nucleation surface of NCD films is investigated for the first time. In particular, the nucleation surface is shown to be susceptible to higher wear compared to the growth surface due to its higher grain boundary line density.

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“…TNF-dependent phosphorylation relies on the correct localization of kinases and their substrates and requires subcellular protein translocation (Micheau and Tschopp, 2003). TNF binding to its receptor recruits a range of complex members to the plasma membrane and binding of TRAF2, and requirement of TRADD, RIPK1, IAPs, and the LUBAC complex for proper activation of TAK1 is well documented (Brenner and Shenderova, 2015). However, the impact of phosphorylation on protein localization is less explored.…”

Section: Resultsmentioning

confidence: 99%

Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling

Mann

Hornung²,

Stafford³

et al. 2020

Preprint

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Tumor necrosis factor (TNF) is one of the few cytokines successfully targeted by therapies against inflammatory diseases. However, blocking this well studied and pleiotropic ligand can cause dramatic side-effects. We reasoned that a systems-level proteomic analysis of TNF signaling could dissect its diverse functions and offer a base for developing more targeted therapies. Combining phosphoproteomics time course experiments with subcellular localization and kinase inhibitor analysis identifies functional modules of phosphorylations. The majority of regulated phosphorylations could be assigned to an upstream kinase by inhibiting master kinases and spatial proteomics revealed phosphorylation-dependent translocations of hundreds of proteins upon TNF stimulation. Phosphoproteome analysis of TNF-induced apoptosis and necroptosis uncovered a key role for transcriptional cyclin-dependent kinase (CDK) activity to promote cytokine production and prevent excessive cell death downstream of the TNF signaling receptor. Our comprehensive interrogation of TNF induced pathways and sites can be explored at http://tnfviewer.biochem.mpg.de/ .

show abstract

Theory and modelling of diamond fracture from an atomic perspective

Cited by 11 publications

References 41 publications

Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling

Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling

Effect of Boron Doping on the Wear Behavior of the Growth and Nucleation Surfaces of Micro- and Nanocrystalline Diamond Films

Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling

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