Results 91 to 100 of about 4,561,775 (254)

Structure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic Mutations

open access: yesPLoS ONE, 2013
Polycomb repressive complex 2 (PRC2) is an important regulator of cellular differentiation and cell type identity. Overexpression or activating mutations of EZH2, the catalytic component of the PRC2 complex, are linked to hyper-trimethylation of lysine ...
Hong Wu   +11 more
semanticscholar   +1 more source

Tracking protein kinase targeting advances: integrating QSAR into machine learning for kinase-targeted drug discovery

open access: yesFuture Science OA
Protein kinases are vital drug targets, yet designing selective inhibitors is challenging, compounded by resistance and kinome complexity. This review explores Quantitative Structure-Activity Relationship (QSAR) modeling for kinase drug discovery ...
Rand Shahin, Sawsan Jaafreh, Yusra Azzam
doaj   +1 more source

The Urea Carboxylase and Allophanate Hydrolase Activities of Urea Amidolyase Are Functionally Independent [PDF]

open access: yes, 2016
Urea amidolyase (UAL) is a multifunctional biotin-dependent enzyme that contributes to both bacterial and fungal pathogenicity by catalyzing the ATP-dependent cleavage of urea into ammonia and CO2.
Bahler   +48 more
core   +2 more sources

Crystal Structures of the Catalytic Domain of Human Soluble Guanylate Cyclase

open access: yesPLoS ONE, 2013
Soluble guanylate cyclase (sGC) catalyses the synthesis of cyclic GMP in response to nitric oxide. The enzyme is a heterodimer of homologous α and β subunits, each of which is composed of multiple domains.
C. Allerston, F. von Delft, O. Gileadi
semanticscholar   +1 more source

Exploring the Antimicrobial Potential of a Novel Phage-Derived Lytic Protein Against Pseudomonas aeruginosa

open access: yesCurrent Issues in Molecular Biology
The escalation of bacterial resistance to existing antibiotics represents a growing global health challenge, exacerbated by the widespread misuse of antimicrobial agents.
Sibongile Mtimka   +9 more
doaj   +1 more source

Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1

open access: yesMolecules, 2017
Allosteric communication among domains in modular proteins consisting of flexibly linked domains with complimentary roles remains poorly understood. To understand how complementary domains communicate, we have studied human Pin1, a representative modular
Jing Wang   +5 more
doaj   +1 more source

Expression of the C-terminal family 22 carbohydratebinding module of xylanase 10B of Clostridium themocellum in tobacco plant [PDF]

open access: yes, 2009
Carbohydrate-binding modules have been shown to alter plant cell wall structural architecture. Hence, they have the potential application of being used to engineer the plant to produce tailor-made natural fibers in the cell wall.
Obembe, Olawole O.
core   +2 more sources

The cysteine protease TcCYSPR04 T. cacao accumulates in senescent leaves and change the biotrophic phase for saprophytic tissues infected by M. perniciosa [PDF]

open access: yes, 2011
A cysteine proteinase named TcCYSPR04 was identified in a cDNA library of the Theobroma cacao-Moniliophthora perniciosa interaction, in the ESTtik-CIRAD database and in the cacao genome of MARS. TcCYSPR04 presents an ORF of 1068 bp encoding protein with:
Cardoso, Thyago Hermylly Santana   +5 more
core  

The Endoplasmic Reticulum Glucosyltransferase Recognizes Nearly Native Glycoprotein Folding Intermediates [PDF]

open access: yes, 2004
The UDP-Glc:glycoprotein glucosyltransferase (GT), a key player in the endoplasmic reticulum (ER) quality control of glycoprotein folding, only glucosylates glycoproteins displaying non-native conformations.
Caramelo, Julio Javier   +3 more
core   +1 more source

The catalytic domain of MMP‐1 studied through tagged lanthanides

open access: yesFEBS Letters, 2012
Pseudocontact shifts (pcs) and paramagnetic residual dipolar couplings (rdc) provide structural information that can be used to assess the adequacy of a crystallographic structure to represent the solution structure of a protein.
I. Bertini   +8 more
semanticscholar   +1 more source

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