Proline-rich salivary proteins have extended conformations. - Wikidata - wikimedia - TriplyDB

Proline-rich salivary proteins have extended conformations.

Proline-rich salivary proteins have extended conformations.

http://www.wikidata.org/entity/Q42567400

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Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion Structural characterization of gephyrin by AFM and SAXS reveals a mixture of compact and extended states Probing the average local structure of biomolecules using small-angle scattering and scaling laws.What interactions drive the salivary mucosal pellicle formation?Cellulase linkers are optimized based on domain type and function: insights from sequence analysis, biophysical measurements, and molecular simulation.Distinct roles for carbohydrate-binding modules of glycoside hydrolase 10 (GH10) and GH11 xylanases from Caldicellulosiruptor sp. strain F32 in thermostability and catalytic efficiency.Characterization of lacrimal proline-rich protein 4 (PRR4) in human tear proteome.Theoretical design of a new chimeric protein for the treatment of breast cancer.Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering.How random are intrinsically disordered proteins? A small angle scattering perspective.Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery.Salivary proline-rich protein may reduce tannin-iron chelation: a systematic narrative review.The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins.Susceptibility to dental caries and the salivary proline-rich proteins Conformational switch of harmonin, a submembrane scaffold protein of the hair cell mechanoelectrical transduction machinery.Hill coefficients of dietary polyphenolic enzyme inhibitiors: can beneficial health effects of dietary polyphenols be explained by allosteric enzyme denaturing?Photodissociation and dissociative photoionization mass spectrometry of proteins and noncovalent protein-ligand complexes.Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering.SEC-SAXS and HDX-MS: A powerful combination. The case of the calcium-binding domain of a bacterial toxin.Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering.Molecular Features Underlying the Perception of Astringency as Probed by Molecular Modeling.PRR4: A novel downregulated gene in laryngeal cancer.Novel Insights from Comparative In Silico Analysis of Green Microalgal Cellulases.Oral Mucosa: Physiological and Physicochemical Aspects

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P2860

Proline-rich salivary proteins have extended conformations.

http://www.wikidata.org/entity/Q42567400

description

2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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2010年论文

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2010年论文

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name

Proline-rich salivary proteins have extended conformations.

@en

Proline-rich salivary proteins have extended conformations.

@nl

type

label

Proline-rich salivary proteins have extended conformations.

@en

Proline-rich salivary proteins have extended conformations.

@nl

prefLabel

Proline-rich salivary proteins have extended conformations.

@en

Proline-rich salivary proteins have extended conformations.

@nl

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J.BPJ.2010.04.050

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Biophysical Journal

P1476

Proline-rich salivary proteins have extended conformations.

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P2093

Aude Vernhet

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Bernard Cabane

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Dominique Durand

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Hélène Boze

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Javier Pérez

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Pascale Sarni-Manchado

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Thérèse Marlin

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Véronique Cheynier

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P2860

Intrinsically unstructured proteins and their functions

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

Structure and bacterial receptor activity of a human salivary proline-rich glycoprotein

Masticatory lubrication. The role of carbohydrate in the lubricating property of a salivary glycoprotein-albumin complex

Global rigid body modeling of macromolecular complexes against small-angle scattering data

PRB1, PRB2, and PRB4 coded polymorphisms among human salivary concanavalin-A binding, II-1, and Po proline-rich proteins

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Intrinsically disordered protein

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

Natively unfolded proteins: a point where biology waits for physics

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