Formaldehyde cross-linking and structural proteomics: Bridging the gap

Srinivasa, Savita; Ding, Xuan; Kast, Juergen

doi:10.1016/j.ymeth.2015.05.006

Cited by 28 publications

(20 citation statements)

References 67 publications

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“…The average value of parameter α estimated from Equations and was 1, which meant that 1 mole of water was produced from the reaction related as Equation while 1 mole of formaldehyde was consumed. This demonstrated that the formaldehyde exhibited an action of bridge connection in the synthesis of the complex:

C_{3} H_{7} N O_{2} S + x C H_{2} O \to c o m p l e x + a x H_{2} O

\frac{7 + 2 x - 2 a x}{12.01 \times (3 + x)} = \frac{5.28 %}{37.27 %}

\frac{7 + 2 x - 2 a x}{14.0037} = \frac{5.28 %}{10.16 %}

…”

Section: Resultsmentioning

confidence: 93%

“…The average value of parameter α estimated from Equations (4) and (5) was 1, which meant that 1 mole of water was produced from the reaction related as Equation (3) while 1 mole of formaldehyde was consumed. This demonstrated that the formaldehyde exhibited an action of bridge connection in the synthesis of the complex: [41] → In addition, the element analysis of the complex surface points ( Figure 3a) was conducted using EDS to investigate the sulphur distribution, and the results are shown in Figure 3b and Table 2. As can be seen from Figure 3b, the X-ray intensity of potassium observed was weak, and the complex surface was mainly composed of carbon, sulphur, nitrogen, and oxygen and not hydrogen.…”

Section: Elemental Analysismentioning

confidence: 99%

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Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO₂ capture

Guo

Fan

et al. 2019

Can J Chem Eng

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This work focused on the preparation and characterization of cysteine‐formaldehyde cross‐linked complex derived from cysteine hydrochloride and formaldehyde. The cross‐linked complex was prepared based on the nucleophilic substitution reaction of cysteine with formaldehyde accompanied by π bond breakage of carbonyl from formaldehyde. Meanwhile, its surface morphology, element composition, group distribution, and thermodynamics were experimentally investigated by means of SEM, XRD, EA, EDS, 1H‐NMR, FTIR, BET, and TGA as well as an analysis of the characteristics of CO2 adsorption. The results indicated that the as‐prepared cross‐linked complex exhibited a rod‐shaped hollow crystal structure with a lateral distribution of sulphur and nitrogen atoms toward the crystal surface. As a mesoporous crystal material, the cross‐linked complex presented a four‐step (amide forming, fast pyrolysis, slow pyrolysis, and dehydrogenation) pyrolysis above 430 K, yet possessed a relatively acceptable thermodynamic stability below 430 K. In addition, the interaction mechanism between the cysteine hydrochloride and formaldehyde was revealed by characteristics and simulation.

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C_{3} H_{7} N O_{2} S + x C H_{2} O \to c o m p l e x + a x H_{2} O

\frac{7 + 2 x - 2 a x}{12.01 \times (3 + x)} = \frac{5.28 %}{37.27 %}

\frac{7 + 2 x - 2 a x}{14.0037} = \frac{5.28 %}{10.16 %}

…”

Section: Resultsmentioning

confidence: 93%

Section: Elemental Analysismentioning

confidence: 99%

Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO₂ capture

Guo

Fan

et al. 2019

Can J Chem Eng

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show abstract

“…[19] Such intermediates are also knownt or eact with Arg, Tyr, His, Trp, and Gln residues to result in protein-protein conjugates. [20] We observedm ultiple unidentified adducts upon incubating ap rotein with 50-100 equivalents of formaldehyde. However,a ll of them were found to be reversible during dialysis and do not inhibit or alter the course of the reaction.…”

mentioning

confidence: 78%

Site‐Selective Labeling of Native Proteins by a Multicomponent Approach

Chilamari

Purushottam

Rai

2017

Chemistry A European J

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Chemical functionalization of proteins is an indispensable tool. Yet, selective labeling of native proteins has been an arduous task. The limited success of chemical methods allows N-terminus protein labeling, but the examples with side-chain residues are rare. Herein, we surpass this challenge through a multicomponent transformation that operates under physiological conditions in the presence of a protein, aldehyde, acetylene, and Cu-ligand complex. The methodology results in the labeling of a single lysine residue in nine distinct proteins.

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“…Stable cells were briefly cross-linked with formaldehyde before harvesting to preserve in vivo interactions of proteins with bio-EGFP and bio-cCE (16). As proof of principle, cytoplasmic proteins recovered on streptavidin paramagnetic beads were visualized by SDS-PAGE and Coomassie Blue staining (Fig.…”

Section: Identification Of Cce-interacting Proteinsmentioning

confidence: 99%

RNA-binding proteins and heat-shock protein 90 are constituents of the cytoplasmic capping enzyme interactome

Trotman

Agana

Giltmier

et al. 2018

Journal of Biological Chemistry

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The -methylguanosine cap is added in the nucleus early in gene transcription and is a defining feature of eukaryotic mRNAs. Mammalian cells also possess cytoplasmic machinery for restoring the cap at uncapped or partially degraded RNA 5' ends. Central to both pathways is capping enzyme (CE) (RNA guanylyltransferase and 5'-phosphatase (RNGTT)), a bifunctional, nuclear and cytoplasmic enzyme. CE is recruited to the cytoplasmic capping complex by binding of a C-terminal proline-rich sequence to the third Src homology 3 (SH3) domain of NCK adapter protein 1 (NCK1). To gain broader insight into the cellular context of cytoplasmic recapping, here we identified the protein interactome of cytoplasmic CE in human U2OS cells through two complementary approaches: chemical cross-linking and recovery with cytoplasmic CE and protein screening with proximity-dependent biotin identification (BioID). This strategy unexpectedly identified 66 proteins, 52 of which are RNA-binding proteins. We found that CE interacts with several of these proteins independently of RNA, mediated by sequences within its N-terminal triphosphatase domain, and we present a model describing how CE-binding proteins may function in defining recapping targets. This analysis also revealed that CE is a client protein of heat shock protein 90 (HSP90). Nuclear and cytoplasmic CEs were exquisitely sensitive to inhibition of HSP90, with both forms declining significantly following treatment with each of several HSP90 inhibitors. Importantly, steady-state levels of capped mRNAs decreased in cells treated with the HSP90 inhibitor geldanamycin, raising the possibility that the cytotoxic effect of these drugs may partially be due to a general reduction in translatable mRNAs.

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Formaldehyde cross-linking and structural proteomics: Bridging the gap

Cited by 28 publications

References 67 publications

Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO₂ capture

Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO₂ capture

Site‐Selective Labeling of Native Proteins by a Multicomponent Approach

RNA-binding proteins and heat-shock protein 90 are constituents of the cytoplasmic capping enzyme interactome

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Formaldehyde cross-linking and structural proteomics: Bridging the gap

Cited by 28 publications

References 67 publications

Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO2 capture

Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO2 capture

Site‐Selective Labeling of Native Proteins by a Multicomponent Approach

RNA-binding proteins and heat-shock protein 90 are constituents of the cytoplasmic capping enzyme interactome

Contact Info

Product

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Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO₂ capture

Preparation and characterization of cysteine‐formaldehyde cross‐linked complex for CO₂ capture