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Carla P. Guimaraes

Researcher at Massachusetts Institute of Technology

Publications -  27
Citations -  5838

Carla P. Guimaraes is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Sortase & Sortase A. The author has an hindex of 21, co-authored 27 publications receiving 5168 citations.

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Site-specific N-terminal labeling of proteins using sortase-mediated reactions

TL;DR: This protocol describes the use of sortase-mediated reactions to label the N terminus of any given protein of interest with a variety of probes such as fluorophores, biotin or even to other proteins.
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Global gene disruption in human cells to assign genes to phenotypes by deep sequencing

TL;DR: This work uses a retroviral gene-trap vector to generate insertions in >98% of the genes expressed in a human cancer cell line that is haploid for all but one of its chromosomes to identify 743 mutations distributed over 12 human genes important for intoxication by four different CDTs.

Global gene disruption in human cells to assign genes to phenotypes

TL;DR: Ploegh et al. as mentioned in this paper developed a mutagenesis-based screening approach in human cells using insertional mutagenisation in KBM7 cells, a chronic myeloid leukemia cell line that is haploid for all chromosomes except chromosome 81.
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Sortase-mediated modification of αDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes

TL;DR: Stochichiometric site-specific labeling on a scale not easily achievable by genetic fusions is demonstrated and introduction of a labile dipeptide linker at the N terminus of a T-cell epitope improves proteasome-dependent class I MHC-restricted peptide cross-presentation when delivered by αDEC205 in vitro and in vivo.
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Sortase A as a tool for high-yield histatin cyclization

TL;DR: A novel and efficient cyclization method that uses the peptidyl‐transferase activity of the Staphylococcus aureus enzyme sortase A to cyclize linear synthetic precursor peptides to provide a general method for easy and efficient manufacturing of large cyclic peptides.