Jan Kosiński
Kosinski, Jan
VIAF ID: 7852158915906950000002 (Personal)
Permalink: http://viaf.org/viaf/7852158915906950000002
Preferred Forms
- 100 0 _ ‡a Jan Kosiński
- 100 1 _ ‡a Kosinski, Jan
4xx's: Alternate Name Forms (13)
5xx's: Related Names (4)
- 510 2 _ ‡a European Molecular Biology Laboratory ‡4 affi ‡4 https://d-nb.info/standards/elementset/gnd#affiliation ‡e Affiliation
- 551 _ _ ‡a Hamburg ‡4 ortw ‡4 https://d-nb.info/standards/elementset/gnd#placeOfActivity
- 551 _ _ ‡a Heidelberg ‡4 ortw ‡4 https://d-nb.info/standards/elementset/gnd#placeOfActivity
- 510 2 _ ‡a Università degli studi di Roma ‡4 affi ‡4 https://d-nb.info/standards/elementset/gnd#affiliation ‡e Affiliation
Works
Title | Sources |
---|---|
AlphaPulldown—a python package for protein–protein interaction screens using AlphaFold-Multimer | |
Analysis of the quaternary structure of the MutL C-terminal domain | |
Artificial intelligence reveals nuclear pore complexity | |
Automated structure modeling of large protein assemblies using crosslinks as distance restraints | |
FRankenstein becomes a cyborg: the automatic recombination and realignment of fold recognition models in CASP6. | |
A ?FRankenstein's monster? approach to comparative modeling: Merging the finest fragments of Fold-Recognition models and iterative model refinement aided by 3D structure evaluation | |
From the resolution revolution to evolution: structural insights into the evolutionary relationships between vesicle coats and the nuclear pore | |
Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle. | |
Identification of Lynch syndrome mutations in the MLH1-PMS2 interface that disturb dimerization and mismatch repair | |
Identifying an interaction site between MutH and the C-terminal domain of MutL by crosslinking, affinity purification, chemical coding and mass spectrometry | |
Improving your target-template alignment with MODalign | |
In-cell architecture of the nuclear pore and snapshots of its turnover | |
Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains | |
A model of restriction endonuclease MvaI in complex with DNA: a template for interpretation of experimental data and a guide for specificity engineering | |
MODexplorer: an integrated tool for exploring protein sequence, structure and function relationships | |
Molecular architecture of the inner ring scaffold of the human nuclear pore complex | |
Molecular basis of tRNA recognition by the Elongator complex | |
Molecular structures of unbound and transcribing RNA polymerase III. | |
Novel protein fold discovered in the PabI family of restriction enzymes | |
The PD-(D/E)XK superfamily revisited: identification of new members among proteins involved in DNA metabolism and functional predictions for domains of (hitherto) unknown function | |
Phylogenetic analysis of haloalkane dehalogenases. | |
Physiological truncation and domain organization of a novel uracil-DNA-degrading factor | |
The PMS2 subunit of human MutLalpha contains a metal ion binding domain of the iron-dependent repressor protein family. | |
Probabilistic cross-link analysis and experiment planning for high-throughput elucidation of protein structure. | |
A short linear motif in scaffold Nup145C connects Y-complex with pre-assembled outer ring Nup82 complex | |
Specialization versus conservation: How Pol I and Pol III use the conserved architecture of the pre-initiation complex for specialized transcription | |
Structure and Evolutionary Origin of Ca2+-Dependent Herring Type II Antifreeze Protein | |
Structure of Prototypic Peptide Transporter DtpA from E. coli in Complex with Valganciclovir Provides Insights into Drug Binding of Human PepT1 | |
Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation | |
Systematic analysis of protein turnover in primary cells. | |
Xlink Analyzer: software for analysis and visualization of cross-linking data in the context of three-dimensional structures |