Author details

Full Name

Ivan Adzhubei

Affiliation

ORCID

Career Start Year

1988

Papers

H Index

Expertise

CM4AI Collaborator

PMID	Paper Title	Journal Title	Published Year
37127568	Small open reading frames: a comparative genetics approach to validation.	BMC Genomics	2023
36305854	Informing variant assessment using structured evidence from prior classifications (PS1, PM5, and PVS1 sequence variant interpretation criteria).	Genet Med	2023
37076482	DeMAG predicts the effects of variants in clinically actionable genes by integrating structural and evolutionary epistatic features.		2023
29388949	A literature review at genome scale: improving clinical variant assessment.	Genet Med	2018
28283406	Transcriptomic insights into genetic diversity of protein-coding genes in X. laevis.	Developmental Biology	2017
25581429	No evidence that selection has been less effective at removing deleterious mutations in Europeans than in Africans.	Nat Genet	2015
23315928	Predicting functional effect of human missense mutations using PolyPhen-2.	Curr Protoc Hum Genet	2013
22555591	Mutation mapping and identification by whole-genome sequencing.	Genome Res	2012
20354512	A method and server for predicting damaging missense mutations.	Nat Methods	2010
19287383	Human mutation rate associated with DNA replication timing.	Nat Genet	2009
18639657	Protein identification pipeline for the homology-driven proteomics.	J Proteomics	2008
19096535	Erratum.	PLoS Genet	2008
18558732	Separating the wheat from the chaff: unbiased filtering of background tandem mass spectra improves protein identification.	J Proteome Res	2008
17571346	Identification and analysis of functional elements in 1% of the human genome by the ENCODE pilot project.	Nature	2007
15660107	A universal trend of amino acid gain and loss in protein evolution.	Nature	2005
9847198	ISSD Version 2.0: taxonomic range extended.	Nucleic Acids Res	1999
9399866	An Integrated Sequence-Structure Database incorporating matching mRNA sequence, amino acid sequence and protein three-dimensional structure data.	Nucleic Acids Res	1998
8980124	Non-random usage of 'degenerate' codons is related to protein three-dimensional structure.	FEBS Lett	1996
8075392	Melting of the left-handed helical conformation of charged poly-L-lysine.	Biopolymers	1994
8381285	Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation.		1993
1628745	Natural polypeptides in left-handed helical conformation. A circular dichroism study of the linker histones' C-terminal fragments and beta-endorphin.	FEBS Letters	1992
1472564	[Study of the conformational properties of C-terminal fragments of histones H1, H5, and beta-endorphin by circular dichroism].	Biofizika	1992
1799404	Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a contranslational protein-folding model.	J Protein Chem	1991
2742922	[Role of the code redundancy in determining cotranslational protein folding].	Biokhimiia	1989
2752893	[Frequency of using codons in mRNA and coding of the domain structure of proteins].	Dokl Akad Nauk SSSR	1989
2765585	[Microcalorimetric study of polypeptides in the conformation of the left helix of the poly-L-proline II type].	Biofizika	1989
3250842	[Role of the rare codon clusters in defining the boundaries of polypeptide chain regions with identical secondary structures in the process of co-translational folding of proteins].	Dokl Akad Nauk SSSR	1988