K
Krzysztof Ginalski
Researcher at University of Texas Southwestern Medical Center
Publications - 22
Citations - 1568
Krzysztof Ginalski is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Peptide sequence & Protein structure. The author has an hindex of 17, co-authored 22 publications receiving 1470 citations. Previous affiliations of Krzysztof Ginalski include Lawrence Livermore National Laboratory & University of Warsaw.
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Journal ArticleDOI
Biochemical identification of Argonaute 2 as the sole protein required for RNA-induced silencing complex activity
TL;DR: The biochemical purification of RISC activity to homogeneity from Drosophila Schnieder 2 cell extracts is reported and homology between the PIWI domain of Ago-2 and endonuclease V is found and potential active-site amino acid residues within the PI WI domain of Argonaute 2 are identified.
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SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family.
Alexander Dikiy,Sergey V. Novoselov,Dmitri E. Fomenko,Aniruddha Sengupta,Bradley A. Carlson,Ronald L. Cerny,Krzysztof Ginalski,Krzysztof Ginalski,Nick V. Grishin,Dolph L. Hatfield,Vadim N. Gladyshev +10 more
TL;DR: A new protein family is defined that includes mammalian selenoproteins SelW, SelV, SelT and SelH, bacterial SelW-like proteins and cysteine-containing proteins of unknown function in all three domains of life, and a mechanism for redox regulation of the 14-3-3 family of proteins is suggested.
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Practical lessons from protein structure prediction
TL;DR: This paper gives an overview of the currently available practical approaches to protein structure prediction capable of generating accurate fold assignment and recent advances in assessment of the prediction quality.
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Determinants in nuclease specificity of ape1 and ape2, human homologues of Escherichia coli exonuclease III
TL;DR: It is found that substitutions in the hydrophobic pocket of Ape1 reduce abasic incision potency about fourfold to 450,000-fold, while introduction of an ExoIII-like pocket into Ape2 enhances its AP endonuclease function.
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A comprehensive update of the sequence and structure classification of kinases
TL;DR: Structural annotations of all kinase families are now revealed, including fold descriptions for all globular kinases, making this the first large functional class of proteins with a comprehensive structural annotation.