J. Yadav

发表

Isolation and characterization of amyloid-like protein aggregates from soya beans and the effect of low pH and heat treatment on their stability.

Charis M. Galanakis, C. Galanakis, Shweta Malik, 2022, Journal of food biochemistry.

Aggregation hot spots in the SARS-CoV-2 proteome may constitute potential therapeutic targets for the suppression of the viral replication and multiplication

Shalini Gour, J. Yadav, 2021, Journal of proteins and proteomics.

Structural basis of β-amyloid-dependent synaptic dysfunctions.

K. Reymann, M. Fändrich, O. Ohlenschläger, 2012, Angewandte Chemie.

Innovative protein and enzyme engineering processes for the production of biomass hydrolyzing enzymes

J. Yadav, Aparna Satapathy, 2022, Biomass, Biofuels, Biochemicals.

A Review on Smart Nanoparticles Drug Delivery System for Targeted Genes

B. Kaur, V. Dubey, J. Yadav, 2020 .

Structural and functional swapping of amyloidogenic and antimicrobial peptides: Redefining the role of amyloidogenic propensity in disease and host defense

J. Yadav, 2021, Journal of peptide science : an official publication of the European Peptide Society.

Mechanisms of Transthyretin Inhibition of β-Amyloid Aggregation In Vitro

P. Wright, Xin Zhang, J. Kelly, 2013, The Journal of Neuroscience.

Impact of semen-derived amyloid (SEVI) on sperm viability and motility: its implication in male reproductive fitness

J. K. Yadav, Pradeep G. Kumar, Vijay Kumar, 2019, European Biophysics Journal.

A differential behavior of α-amylase, in terms of catalytic activity and thermal stability, in response to higher concentration CaCl2.

J. Yadav, 2012, International journal of biological macromolecules.

Management of Alzheimer’s Disease with nutraceuticals

J. Yadav, 2021 .

Thermal stability of α-amylase in aqueous cosolvent systems

V. Prakash, J. Yadav, 2009, Journal of Biosciences.

Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM

K. Lasker, N. Grigorieff, A. Rohou, 2015, Proceedings of the National Academy of Sciences.

Enhanced Fibril Fragmentation of N-Terminally Truncated and Pyroglutamyl-Modified Aβ Peptides.

M. Fändrich, J. Balbach, J. Rahfeld, 2016, Angewandte Chemie.

Structure and biomedical applications of amyloid oligomer nanoparticles.

M. Fändrich, T. Simmet, T. Aumüller, 2014, ACS nano.

Amyloid cross-sequence interaction between Aβ(1-40) and αA(66-80) in relation to the pathogenesis of cataract.

J. Yadav, A. Schimansky, 2021, International journal of biological macromolecules.

Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen

W. Greene, F. Kirchhoff, K. Nilsson, 2014, Nature Communications.

Effect of non aqueous solvent on structural stability of α-amylase: A cost-effective prospective for protein stabilization

J. Chauhan, W. Kapfo, J. Yadav, 2013 .

Structure, function and antagonism of semen amyloids.

J. Münch, M. Fändrich, N. Roan, 2018, Chemical communications.

TARGETING THE SEMEN DERIVED AMYLOIDS TO CONTROL HIV TRANSMISSION: PERSPECTIVES AND CHALLENGES

Vijay Kumar, Shalini Gour, J. Yadav, 2016 .

Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens.

J. K. Yadav, Vijay Kumar, Shalini Gour, 2020, International journal of biological macromolecules.

Pheromone peptide cOB1 from native Enterococcus faecalis forms amyloid‐like structures: A new paradigm for peptide pheromones

Vijay Kumar, M. Rana, Shalini Gour, 2019, Journal of peptide science : an official publication of the European Peptide Society.

Mammalian antimicrobial peptide protegrin‐4 self assembles and forms amyloid‐like aggregates: Assessment of its functional relevance

J. Pandey, Rajanish Giri, Kundlik Gadhave, 2019, Journal of peptide science : an official publication of the European Peptide Society.

Antimicrobial peptide (Cn‐AMP2) from liquid endosperm of Cocos nucifera forms amyloid‐like fibrillar structure

Priyanka Bhat, Vijay Kumar, Shalini Gour, 2016, Journal of peptide science : an official publication of the European Peptide Society.

Macromolecular Crowding Enhances Catalytic Efficiency and Stability of α-Amylase

J. Yadav, 2012, ISRN biotechnology.

Stabilization of α-Amylase, the Key Enzyme in Carbohydrates Properties Alterations, at Low pH

V. Prakash, J. Yadav, 2011 .

Discerning Modulation of α-Synuclein Amyloid Assembly by α-Crystallin.

P. Chaudhuri, K. Rani, J. Yadav, 2023, ACS chemical neuroscience.

Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens

J. K. Yadav, R. Harsolia, Lakshman Ram, 2020, The Protein Journal.

Thermal stability of alpha-amylase in aqueous cosolvent systems.

V. Prakash, J. Yadav, 2009, Journal of biosciences.

Effect of Green Tea Polyphenol Epigallocatechin-3-gallate on the Aggregation of αA(66-80) Peptide, a Major Fragment of αA-crystallin Involved in Cataract Development

J. Pandey, J. K. Yadav, P. Goyal, 2017, Current eye research.

Assessment of the effect of macromolecular crowding on aggregation behaviour of a model amyloidogenic Peptide.

G. Hause, Vijay Kumar, Nimisha Gupta, 2014, Protein and peptide letters.

Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen

W. Greene, F. Kirchhoff, K. Nilsson, 2014, Nature Communications.

Counter effect of sucrose on ethanol-induced aggregation of protein.

J. Chauhan, Jay Kant Yadav, N Chandani, 2010, Protein and peptide letters.

Structure, function and antagonism of semen amyloids.

J. Münch, M. Fändrich, N. Roan, 2018, Chemical communications.

Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM

N. Grigorieff, A. Rohou, M. Fändrich, 2015, Proceedings of the National Academy of Sciences.

Structural basis of β-amyloid-dependent synaptic dysfunctions.

K. Reymann, M. Fändrich, O. Ohlenschläger, 2012, Angewandte Chemie.

The mechanism of phosphatidylcholine‐induced interference of PAP (248‐286) aggregation

J. Pandey, Rajanish Giri, P. M. Mishra, 2019, Journal of peptide science : an official publication of the European Peptide Society.

Macromolecular Crowding Enhances Catalytic Eﬃciency and Stability of 𝛼𝛼 -Amylase

J. Yadav, 2015 .

Computational investigation for modeling the protein–protein interaction of TasA(28–261)–TapA(33–253): a decisive process in biofilm formation by Bacillus subtilis

J. Pandey, N. Verma, J. K. Yadav, 2020, Journal of Molecular Modeling.

Computational investigation for modelling the protein-protein interaction of TasA(28-261) – TapA(33-253): a decisive process in biofilm formation by Bacillus subtilis

J. Pandey, N. Verma, P. Goyal, 2020, bioRxiv.