Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. (Q34462209)

2 August 2017

Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. (English)

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2 August 2017

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Ming-Daw Tsai

5

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Angela Gronenborn

object named as

Angela M Gronenborn

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author name string

In-Ja L Byeon

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2 August 2017

Hongyuan Li

2

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2 August 2017

Haiyan Song

3

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2 August 2017

1 November 2005

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Nature Structural & Molecular Biology

2 August 2017

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2 August 2017

12

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2 August 2017

987-993

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2 August 2017

11

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https://scigraph.springernature.com/pub.10.1038/nsmb1008

2 August 2017

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cites work

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Ki67 protein: the immaculate deception?

21 January 2018

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The Ki-67 protein: from the known and the unknown

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The cell proliferation-associated antigen of antibody Ki-67: a very large, ubiquitous nuclear protein with numerous repeated elements, representing a new kind of cell cycle-maintaining proteins

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The biochemical characterization of the DNA binding activity of pKi67.

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The Ki-67 protein interacts with members of the heterochromatin protein 1 (HP1) family: a potential role in the regulation of higher-order chromatin structure

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Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53

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The FHA domain is a modular phosphopeptide recognition motif.

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The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms

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Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9

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NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase

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SMART, a simple modular architecture research tool: identification of signaling domains

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The forkhead-associated domain of Ki-67 antigen interacts with the novel kinesin-like protein Hklp2

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A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis

21 January 2018

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Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions

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Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae.

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Replication Checkpoint Protein Mrc1 Is Regulated by Rad3 and Tel1 in Fission Yeast

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Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling

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Nibrin forkhead-associated domain and breast cancer C-terminal domain are both required for nuclear focus formation and phosphorylation

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Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate

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Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2

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Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53

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Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexes

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Isotope-filtered 2D NMR of a protein-peptide complex: study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin

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Posttranslational modifications of the KI-67 protein coincide with two major checkpoints during mitosis

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Phosphorylation of sites 3a and 3b (Ser640 and Ser644) in the control of rabbit muscle glycogen synthase

31 March 2020

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FHA domain-ligand interactions: importance of integrating chemical and biological approaches

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31 March 2020

Identifiers

DOI

10.1038/NSMB1008

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Dimensions Publication ID

2 August 2017

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