Results 61 to 70 of about 1,964,169 (255)

Reconstructing enzyme evolution by protein engineering

open access: yesFEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler   +2 more
wiley   +1 more source

Cloning and phenotypic expression in Escherichia coli of a Bacillus subtilis gene fragment coding for sucrose hydrolysis [PDF]

open access: yes, 1986
Friehs K, Schörgendorfer K, Schwab H, Lafferty RM. Cloning and phenotypic expression in Escherichia coli of a Bacillus subtilis gene fragment coding for sucrose hydrolysis. Journal of Biotechnology.
Lafferty, R. M.   +3 more
core   +1 more source

Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]

open access: yes, 2006
In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, T., Maier, Tobias
core   +1 more source

Cloning, Expression, and Purification of α, βa, and βb Subunits of Human Inhibin Protein in Escherichia coli

open access: yesMajallah-i Dānishgāh-i ̒Ulūm-i Pizishkī-i Qum, 2018
Background and Objectives: Inhibin is a glycoprotein hormone commonly found in the circulation, but its level increases in some diseases, and its measurement by serological method using anti-inhibin monoclonal antibodies, can help in diagnosis of some ...
Mohammad Ataei   +4 more
doaj  

Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions

open access: yesFEBS Letters, EarlyView.
The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang   +4 more
wiley   +1 more source

Cloning of BMP-2 Gene and Its Expression Study in E. coli in Order to Produce a Recombinant Drug

open access: yesپزشکی بالینی ابن سینا, 2014
Introduction & Objective: Bone morphogenetic proteins are a group of cytokines that belongs to superfamily TGFβ. These proteins play an important role in evolution of many of organs and tissues through germinal period followed by amending and rebuilding ...
Nejad Mohammadi   +5 more
doaj  

Heterologous Expression and Purification of the CRISPR-Cas12a/Cpf1 Protein

open access: yesBio-Protocol, 2018
This protocol provides step by step instructions (Figure 1) for heterologous expression of Francisella novicida Cas12a (previously known as Cpf1) in Escherichia coli.
P Mohanraju   +3 more
doaj   +1 more source

Microbiome‐blood–brain barrier interactions in aging — mechanisms and therapeutic potential

open access: yesFEBS Letters, EarlyView.
Aging reshapes the gut microbiome (↓SCFA‐producing commensals; ↑pro‐inflammatory outputs), shifting circulating metabolites (↓SCFAs; ↑LPS, ↑TMAO, ↑PAA) that act at the BBB to increase nonspecific transcytosis, alter transport, and promote astrocyte reactivity, heightening brain vulnerability.
Daniel Cuervo‐Zanatta   +3 more
wiley   +1 more source

Proteomic Analysis of Duodenal Tissue from Escherichia coli F18-Resistant and -Susceptible Weaned Piglets. [PDF]

open access: yesPLoS ONE, 2015
Diarrhea and edema disease in weaned piglets due to infection by Escherichia coli F18 is a leading cause of economic loss in the pig industry. Resistance to E.
Zhengchang Wu   +6 more
doaj   +1 more source

Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins

open access: yesMolecules, 2022
Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins.
Liliana S. O. Silva   +3 more
doaj   +1 more source

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