Concept

Protein family

Related publications (98)

Progress in quantitative single-molecule localization microscopy

Aleksandra Radenovic, Paolo Annibale, Hendrik Georges Deschout, Marco Scarselli, Arun Shivanandan

With the advent of single-molecule localization microscopy (SMLM) techniques, intracellular proteins can be imaged at unprecedented resolution with high specificity and contrast. These techniques can lead to a better understanding of cell functioning, as t ...

Springer2014

From High- to Super-resolution Mass Spectrometry

Yury Tsybin

High-resolution mass spectrometry (MS) is indispensable for the molecular-level analysis of biological and environmental samples with great intra- and inter-molecular complexity. Here, we summarize developments in Fourier transform mass spectrometry (FTMS) ...

Schweizerische Chemische Gesellschaft2014

Empirical multi-dimensional space for scoring peptide spectrum matches in shotgun proteomics

Yury Tsybin, Unige Anna Laskay

Data-dependent tandem mass spectrometry (MS/MS) is one of the main techniques for protein identification in shotgun proteomics. In a typical LC MS/MS workflow, peptide product ion mass spectra (MS/MS spectra) are compared with those derived theoretically f ...

Amer Chemical Soc2014

A Novel Pulse-Chase SILAC Strategy Measures Changes in Protein Decay and Synthesis Rates Induced by Perturbation of Proteostasis with an Hsp90 Inhibitor

Vassily Hatzimanikatis, Julien Racle, Céline Hernández

Standard proteomics methods allow the relative quantitation of levels of thousands of proteins in two or more samples. While such methods are invaluable for defining the variations in protein concentrations which follow the perturbation of a biological sys ...

Public Library of Science2013

Dynamic Impacts of the Inhibition of the Molecular Chaperone Hsp90 on the T-Cell Proteome Have Implications for Anti-Cancer Therapy

Julien Racle, Céline Hernández

The molecular chaperone Hsp90-dependent proteome represents a complex protein network of critical biological and medical relevance. Known to associate with proteins with a broad variety of functions termed clients, Hsp90 maintains key essential and oncogen ...

Public Library of Science2013

Proteome Digestion Specificity Analysis for Rational Design of Extended Bottom-up and Middle-down Proteomics Experiments

Yury Tsybin, Kristina Srzentic, Unige Anna Laskay

Mass spectrometry (MS)-based bottom-up proteomics (BUP) is currently the method of choice for large-scale identification and characterization of proteins present in complex samples, such as cell lysates, body fluids, or tissues. Technically, BUP relies on ...

Amer Chemical Soc2013

Prion versus Doppel Protein Misfolding: New Insights from Replica-Exchange Molecular Dynamics Simulations

Ursula Röthlisberger, Ivano Tavernelli

The doppel (Dpl) and prion (PrP) proteins share a very similar fold (three helices and two short beta-strands), while they differ significantly in sequence (only 25% homologous) and in disease-related beta-rich conformations that occur for PrP only. In a p ...

American Chemical Society2013

Enlightening G-protein-coupled receptors on the plasma membrane using super-resolution photoactivated localization microscopy

Aleksandra Radenovic, Paolo Annibale, Marco Scarselli

The possibility to visualize and image the arrangement of proteins within the cell at the molecular level has always been an attraction for scientists in biological research. In particular, for signalling molecules such as GPCRs (G-protein-coupled receptor ...

Portland Press2013

Top-down analysis of 30–80 kDa proteins by electron transfer dissociation time-of-flight mass spectrometry

Yury Tsybin, Luca Fornelli, Julien Parra

Electron transfer dissociation (ETD)-based top-down mass spectrometry (MS) is the method of choice for in-depth structure characterization of large peptides, small- and medium-sized proteins, and non-covalent protein complexes. Here, we describe the perfor ...

Springer Berlin Heidelberg2013

GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP

Paolo De Los Rios, Pierre Goloubinoff, Vishal Sood, Andrija Finka

Chaperonins are cage-like complexes in which nonnative polypeptides prone to aggregation are thought to reach their native state optimally. However, they also may use ATP to unfold stably bound misfolded polypeptides and mediate the out-of-cage native refo ...

National Academy of Sciences2013

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