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ProteomicsLimited proteolysis-coupled mass spectrometry captures proteome-wide protein structural alterations and biomolecular condensation in living cells
To study protein structures directly within cells, we developed in-cell limited proteolysis-coupled mass spectrometry (in-cell LiP-MS). Conditions for introduction of proteinase K into human cells using electroporation were optimized and validated for intracellular cleavages. In-cell LiP-MS captured...
ORGANISM(S): Homo sapiens (Human) 
2025-11-09 | PXD069095 | Pride
Stress granules Mass spectrometry In-cell lip Structural proteomics Limited proteolysis Arsenite treatment Rapamycin 
ProteomicsProteome-wide structural changes measured with limited proteolysis-mass spectrometry: an advanced protocol for high-throughput applications.
Proteins regulate biological processes by changing their structure or abundance to accomplish a specific function. In response to any perturbation or stimulus, protein structure may be altered by a variety of molecular events, such as post translational modification, protein-protein interaction, agg...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-01-10 | PXD031627 | Pride
Alpha-synuclein Shotgun proteomics Yeast Structural proteomics Lip-ms 
ProteomicsFLiPPR: A Processor for Limited Proteolysis (LiP) Mass Spectrometry Datasets Built on FragPipe
Here, we present FLiPPR, or FragPipe LiP (limited proteolysis) Processor, a tool that facilitates the analysis of data from limited proteolysis mass spectrometry (LiP-MS) experiments following primary search and quantification in FragPipe. LiP-MS has emerged as a method that can provide proteome-wid...
ORGANISM(S): Bacillus cereus (strain ATCC 14579 / DSM 31) 
2024-05-24 | PXD047776 | Pride
Data processing Proteomics Limited proteolysis Bacillus cereus atcc 14579 Bacilli Mass spectrometry Bioinformatics Bottom-up Data 
UnknownAnalysis of Limited Proteolysis-Coupled Mass Spectrometry Data.
Not available
S-EPMC12036054 | biostudies-literature
UnknownBenchmarking of Quantitative Proteomics Workflows for Limited Proteolysis Mass Spectrometry.
Not available
S-EPMC12022698 | biostudies-literature
ProteomicsA map of protein-metabolite interactions reveals principles of chemical communication
Application of a novel mass spectrometry-based high-throughput workflow (LiP-SMap) and data resource based on limited proteolysis (LiP) of complex samples. Proteome-wide limited proteolysis sites were obtained in different conditions to infer ligand-induced and protein-protein interaction induced co...
ORGANISM(S): Escherichia coli Saccharomyces cerevisiae (Baker's yeast) 
2018-01-04 | PXD006543 | Pride
Small molecules Limited proteolysis Lip-smap Dia-ms E.coli 
UnknownLimited Proteolysis-Mass Spectrometry Reveals Aging-Associated Changes in Cerebrospinal Fluid Protein Abundances and Structures.
Not available
S-EPMC9893943 | biostudies-literature
UnknownMTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometry.
Not available
S-EPMC3557227 | biostudies-literature
UnknownFLiPPR: A Processor for Limited Proteolysis (LiP) Mass Spectrometry Datasets Built on FragPipe.
Not available
S-EPMC10723326 | biostudies-literature
UnknownFLiPPR: A Processor for Limited Proteolysis (LiP) Mass Spectrometry Data Sets Built on FragPipe.
Not available
S-EPMC11590172 | biostudies-literature
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