Allosteric inhibition of CRISPR-Cas9 by bacteriophage-derived peptides

Autor: Yan-ru Cui, Jun Chen, Shuyue Wang, Biao Jiang, Zhuhong Zhang, Wenzhang Chen, Peixiang Ma, Guang Yang, Bing Meng, Bei Yang, Shao-jie Wang, Wei Zhu, Jie Li, Jia Liu

Publikováno v: Genome Biology
Genome Biology, Vol 21, Iss 1, Pp 1-15 (2020)

Background CRISPR-Cas9 has been developed as a therapeutic agent for various infectious and genetic diseases. In many clinically relevant applications, constitutively active CRISPR-Cas9 is delivered into human cells without a temporal control system.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4876b6e203ea61a90716fec5a1a320ea
https://pubmed.ncbi.nlm.nih.gov/32102684

Mutations in fd phage major coat protein modulate affinity of the displayed peptide

Autor: Valery A. Petrenko, E. S. Pereyaslavskaya, Maria Grishina, A.M. Eroshkin, Vladimir Potemkin, P.K. Jayanna, G.A. Kuzmicheva

Multibillion-clone libraries of phages displaying guest peptides fused to the major coat protein pVIII (landscape libraries) are a rich source of probes for proteinaceous and non-proteinaceous targets. As opposed to the pIII-type fusion phages, which

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f017f6250b8396871b4782e1383b5b5c
https://europepmc.org/articles/PMC2742390/

Transmembrane Segment Peptides of the Ff Phage Major Coat Protein Form Parallel Homodimers

Autor: Charles M. Deber, Roman A. Melnyk, Anthony W. Partridge

Publikováno v: Peptides: The Wave of the Future ISBN: 9789401039055

The Ff filamentous phage major coat protein (MCP) is located in the inner membrane of host cell Escherichia coli prior to assembly into the lipid-free virion. The 50-residue MCP consists of a mobile N-terminal amphipathic helix that is connected by a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::27b84efea42c93f085729f0eb8b5bb43
https://doi.org/10.1007/978-94-010-0464-0_385

Filamentous phage pre-coat is an integral membrane protein: analysis by a new method of membrane preparation

Autor: Marjorie Russel, Peter Model

Publikováno v: Cell. 28(1)

We show, using a simple, rapid fractionation method, that the precursor to the filamentous phage major coat protein is an integral membrane protein. The method, which consists of treatment of Escherichia coli with 0.1 N NaOH followed by centrifugatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::009503d859c0297bdda601a2681d477a
https://pubmed.ncbi.nlm.nih.gov/7066983

Monoclonal antibodies that recognise filamentous phage: tools for phage display technology

Autor: Gianni Cesareni, Luciana Dente, Paola Delmastro, Paolo Monaci, Gioacchino Micheli, Antonella Folgori, Alessandra Luzzago, Franco Felici, Alfredo Nicosia

Publikováno v: Università di Pisa-IRIS
Gene (Amst.) 148 (1994): 7–13. doi:10.1016/0378-1119(94)90227-5
info:cnr-pdr/source/autori:Dente, Luciana; Cesareni, Gianni; Micheli, Gioacchino; Felici, Franco; Folgori, Antonella; Luzzago, Alessandra; Monaci, Paolo; Nicosia, Alfredo L.; Delmastro, Paola/titolo:Monoclonal antibodies that recognise filamentous phage: tools for phage display technology/doi:10.1016%2F0378-1119(94)90227-5/rivista:Gene (Amst.)/anno:1994/pagina_da:7/pagina_a:13/intervallo_pagine:7–13/volume:148

We generated six hybridoma cell lines that secrete monoclonal antibodies (mAb) which specifically bind filamentous phage coat proteins. Two of these mAb recognise epitopes that include the N terminus of the coat protein III (pIII), while two others a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6016f10b667b7475d47e7f133fcf6df
https://arpi.unipi.it/handle/11568/23050