Single-cell imaging mass spectrometry

Passarelli, Melissa K.; Ewing, Andrew G.

doi:10.1016/j.cbpa.2013.07.017

Cited by 98 publications

(88 citation statements)

References 46 publications

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“…These molecular events can thus be regulated by the prejunctional heteroreceptor complexes through receptorvesicular protein interactions which can involve also the neurotransmitter transporters and actin [126,127]. The pattern and amount of vesicular release of transmitters to be learnt may also lead to changes in the lipid contents of the plasma membrane which can be of relevance for short term memory formation [128]. Thus, lipid messengers exist like lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) and others, which are activators of rhodopsin family GPCRs located in the plasma membrane [129].…”

Section: Role Of Allosteric Receptor-receptor Interactions In Heterormentioning

confidence: 99%

Receptor-receptor interactions in heteroreceptor complexes: a new principle in biology. Focus on their role in learning and memory

Fuxé

Borroto‐Escuela²,

Ciruela³

et al. 2014

Neurosci Discov

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The allosteric receptor-receptor interactions over the interfaces in heteroreceptor complexes have been explored and their biochemical, pharmacological and functional integrative implications in the Central Nervous System (CNS) described. GPCR interacting proteins participate in these complexes mainly through modulation of receptor-receptor interactions. Methodologies to study heteroreceptor complexes in living cells (FRET and BRET-based techniques) and in brain tissue (in situ proximity ligation assay) are briefly summarized. The physiological and pathological relevance of the allosteric receptor-receptor interactions in heteroreceptor complexes is emphasized and novel strategies for treatment of mental and neurological disease are developed based on this new biological principle of integration. The molecular basis of learning and memory is proposed to be based on the reorganization of the homo-and heteroreceptor complexes in the postjunctional membrane of synapses leading also to changes in the prejunctional receptor complexes to facilitate the pattern of transmitter release to be learned. Long-term memory may be created by the transformation of parts of the heteroreceptor complexes into unique transcription factors which can lead to the formation of specific adapter proteins which can consolidate the heteroreceptor complexes into long-lived complexes with conserved allosteric receptor-receptor interactions.

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Section: Role Of Allosteric Receptor-receptor Interactions In Heterormentioning

confidence: 99%

Receptor-receptor interactions in heteroreceptor complexes: a new principle in biology. Focus on their role in learning and memory

Fuxé

Borroto‐Escuela²,

Ciruela³

et al. 2014

Neurosci Discov

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“…Advanced laser optics enables high spatial resolution MALDI MS analyses, including MALDI imaging of single cells [47–49]. New detector systems allow for higher molecular weight proteins to be efficiently detected directly from complex environments, including tissue [50].…”

Section: Looking To the Futurementioning

confidence: 99%

Advanced mass spectrometry technologies for the study of microbial pathogenesis

Moore

Caprioli

Skaar

2014

Current Opinion in Microbiology

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Matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) has been successfully applied to the field of microbial pathogenesis with promising results, principally in diagnostic microbiology to rapidly identify bacteria based on the molecular profiles of small cell populations. Direct profiling of molecules from serum and tissue samples by MALDI MS providesa means to study the pathogen-host interaction and to discover potential markers of infection. Systematic molecular profiling across tissue sections represents a new imaging modality, enabling regiospecific molecular measurements to be made in situ, in both two- and three-dimensional analyses. Herein, we briefly summarize work that employs MALDI MS to study the pathogenesis of microbial infection.

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“…Many of the components of these networks have been identified by proteomics (mainly mass spectrometry; Passarelli and Ewing, 2013). However, an immense amount of information is needed to decipher the structure of a myriad of molecular assemblies that comprise the crowded and complex environment of the cell.…”

Section: Introductionmentioning

confidence: 99%

Cellular structural biology as revealed by cryo-electron tomography

Irobalieva

Martins

Medalia

2016

Journal of Cell Science

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Understanding the function of cellular machines requires a thorough analysis of the structural elements that underline their function. Electron microscopy (EM) has been pivotal in providing information about cellular ultrastructure, as well as macromolecular organization. Biological materials can be physically fixed by vitrification and imaged with cryo-electron tomography (cryo-ET) in a close-to-native condition. Using this technique, one can acquire three-dimensional (3D) information about the macromolecular architecture of cells, depict unique cellular states and reconstruct molecular networks. Technical advances over the last few years, such as improved sample preparation and electron detection methods, have been instrumental in obtaining data with unprecedented structural details. This presents an exciting opportunity to explore the molecular architecture of both individual cells and multicellular organisms at nanometer to subnanometer resolution. In this Commentary, we focus on the recent developments and in situ applications of cryo-ET to cell and structural biology.

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Single-cell imaging mass spectrometry

Cited by 98 publications

References 46 publications

Receptor-receptor interactions in heteroreceptor complexes: a new principle in biology. Focus on their role in learning and memory

Receptor-receptor interactions in heteroreceptor complexes: a new principle in biology. Focus on their role in learning and memory

Advanced mass spectrometry technologies for the study of microbial pathogenesis

Cellular structural biology as revealed by cryo-electron tomography

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