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UnknownElectron-deficient p-benzoyl-l-phenylalanine derivatives increase covalent chemical capture yields for protein-protein interactions.
Not available
S-EPMC6511736 | biostudies-literature
ProteomicsHsp70 and NAC chaperone systems are in close proximity on the ribosome
To understand the orientation of Hsp70 Ssb on the ribosome in living Saccharomyces cerevisiae cells we incorporated the noncanonical, photoactivatable amino acid p-benzoyl-L-phenylalanine (Bpa) in place of specific individual endogenous amino acids in Ssb1. To identify the proteins to which Ssb1Bpa ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-01-08 | PXD046895 | Pride
Nac Ssb1 Ribosome In vivo crosslinking Hsp70 
UnknownDesign and synthesis of a clickable, photoreactive amino acid p-(4-(but-3-yn-1-yl)benzoyl)-l-phenylalanine for peptide photoaffinity labeling.
Not available
S-EPMC9811243 | biostudies-literature
ProteomicsIdentifying peptides and sites involved in FtsZ self-assembly in Escherichia coli through in vivo protein photocrosslinking of FtsZ residues mediated by the unnatural amino acid Bpa (p-benzoyl-L-phenylalanine), followed by tandem mass spectrometry analysis of purified FtsZ crosslinking dimers.
Bacterial cell division hinges on the Z-ring, an architecture built from the dynamical assembly and disassembly of FtsZ proteins. This delicate balance ensures not only apparent stability, but also continuous remodeling, both of which are required for Z-ring functioning. However, the molecular natur...
ORGANISM(S): Escherichia coli 
2025-05-10 | PXD063736 | Pride
Escherichia coli Ftsz Bacterial cell division P-benzoyl-l-phenylalanine Photocrosslinking 
ProteomicsA photo-crosslink approach to identify class II SUMO binders
The small ubiquitin-like modifier (SUMO) is involved in various cellular processes and mediates known non-covalent protein-protein interactions by three distinct binding surfaces, whose interactions are termed class I to class III. While interactors for the class I interaction, which involves bindin...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD033107 | Pride
Ubiquitin-like protein Chemical crosslinking Mass spectrometry Genetic code expansion P-benzoyl-phenylalanine Sumo 
Proteomicsdentification of Cross-linking partners of BpA modified p37 and p97 by photo cross-linking MS
we wanted to see where and how the protein p37 interacts with its partner proteins p97, PPI,Sds22 and I3. To this end p37 derivatives with genetically encoded crosslinking amino acid (p-benzoyl-L-phenylalanine) were generated. After incubation with the partner proteins, photocross-linking and trypt...
ORGANISM(S): Homo sapiens (Human) 
2020-10-19 | PXD021182 | Pride
P37 Ppi Sds22 Photo cross-linking P97 
ProteomicsIdentification of Cross-linking partners of BpA modified p97 by photo cross-linking MS
We wanted to see where and how the protein p97 interacts with its partner proteins p37, PPI,Sds22 and I3. To this end a p97 derivative with genetically encoded crosslinking amino acid (p-benzoyl-L-phenylalanine) was generated. After incubation with the partner proteins, photocross-linking and trypti...
ORGANISM(S): Homo sapiens (Human) 
2023-07-10 | PXD039939 | Pride
Aaa protease Bpa crosslinking P97 
ProteomicsEarly Scanning of Nascent Polypeptides inside the Ribosomal Tunnel by NAC
In this study, NAC was UV-crosslinked using the photo-crosslinking amino acid p-benzoyl-L-phenylalanine (pBPA) in order to determine specific interaction sites of the alphaNAC N-terminus in the native protein structure. Furthermore, quantitative chemical crosslinking coupled to mass spectrometry (q-...
ORGANISM(S): Homo sapiens (Human) Caenorhabditis elegans 
2019-07-25 | PXD011995 | Pride
Nac Structural mass spectrometry Uv-crosslinking Q-xl-ms 
ProteomicsIdentification of HJURP binding determinants on the Mis18 complex using photo-cross-linking and mass spectrometry
In the early G1 phase of the cell cycle, human HJURP is recruited to centromeres by the Mis18 complex, which consists of Mis18α, Mis18β and M18BP1. This interaction of HJURP with the Mis18 complex is essential for CENP-A deposition and the preservation of centromere identity. To identify the binding...
ORGANISM(S): Homo sapiens (Human) 
2019-08-01 | PXD013339 | Pride
Photo-cross-linking Q-exactive Abk Human Kinetochore Centromere Protein complex Bpa Stavrox 
ProteomicsIdentification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry
The 26S proteasome is the endpoint of the ubiquitin-proteasome system, an essential pathway for maintaining cellular homeostasis through targeted degradation of misfolded, damaged, and obsolete proteins. Substrates labeled with ubiquitin are directed to the 26S proteasome by binding to one or more u...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2026-06-08 | PXD075114 | Pride
26s proteasome Ubiquitin Ubiquitin receptors 
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