Results 21 to 30 of about 1,642,696 (345)

Author Correction: The Aurora B specificity switch is required to protect from non-disjunction at the metaphase/anaphase transition

Nature Communications, 2020
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Joanna R. Kelly, Silvia Martini, Nicola Brownlow, Dhira Joshi, Stefania Federico, Shirin Jamshidi, Svend Kjaer, Nicola Lockwood, Khondaker Miraz Rahman, Franca Fraternali, Peter J. Parker, Tanya N. Soliman   +11 more
doaj   +1 more source

A novel RLIM/RNF12 variant disrupts protein stability and function to cause severe Tonne–Kalscheuer syndrome

Scientific Reports, 2021
Tonne–Kalscheuer syndrome (TOKAS) is an X-linked intellectual disability syndrome associated with variable clinical features including craniofacial abnormalities, hypogenitalism and diaphragmatic hernia.
Francisco Bustos, Carmen Espejo-Serrano, Anna Segarra-Fas, Rachel Toth, Alison J. Eaton, Kristin D. Kernohan, Meredith J. Wilson, Lisa G. Riley, Greg M. Findlay   +8 more
doaj   +1 more source

The Aurora B specificity switch is required to protect from non-disjunction at the metaphase/anaphase transition

Nature Communications, 2020
In mitosis, Aurora B switches substrate specificity in response to phosphorylation of S227 in the activation loop by a cell cycle-processed active fragment of PKCε.
Joanna R. Kelly, Silvia Martini, Nicola Brownlow, Dhira Joshi, Stefania Federico, Shirin Jamshidi, Svend Kjaer, Nicola Lockwood, Khondaker Miraz Rahman, Franca Fraternali, Peter J. Parker, Tanya N. Soliman   +11 more
doaj   +1 more source

Pathogenic FAM83G palmoplantar keratoderma mutations inhibit the PAWS1:CK1α association and attenuate Wnt signalling. [version 1; peer review: 2 approved]

Wellcome Open Research, 2019
Background: Two recessive mutations in the FAM83G gene, causing A34E and R52P amino acid substitutions in the DUF1669 domain of the PAWS1 protein, are associated with palmoplantar keratoderma (PPK) in humans and dogs respectively.
Kevin Z.L. Wu, Rebecca A. Jones, Theresa Tachie-Menson, Thomas J. Macartney, Nicola T. Wood, Joby Varghese, Robert Gourlay, Renata F. Soares, James C. Smith, Gopal P. Sapkota   +9 more
doaj   +1 more source

Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry [PDF]

, 2012
Protein phosphorylation is a common post-translational modification in eukaryotic cells and has a wide range of functional effects. Here, we used mass spectrometry to search for phosphorylated residues in all the proteins of influenza A and B viruses ...
Denham, Eleanor M., Fodor, Ervin, Hester, Svenja S., Hutchinson, Edward C., Ridlova, Gabriela, Thomas, Benjamin, Trudgian, David C., Turrell, Lauren, York, Ashley   +8 more
core   +3 more sources

Phosphorylation at the Interface [PDF]

Structure, 2011
Proteomic studies have identified thousands of eukaryotic phosphorylation sites (phosphosites), but few are functionally characterized. Nishi et al., in this issue of Structure, characterize phosphosites at protein-protein interfaces and estimate the effect of their phosphorylation on interaction affinity, by combining proteomics data with protein ...
openaire   +3 more sources

Revisiting Frank–Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr) in a length-dependent fashion [PDF]

, 2016
Force and power in cardiac muscle have a known dependence on phosphorylation of the myosin-associated regulatory light chain (RLC). We explore the effect of RLC phosphorylation on the ability of cardiac preparations to redevelop force (ktr ) in maximally
Abraham, Adhikari, Aoki, Araujo, Barany, Blue, Bremel, Brenner, Brenner, Colson, Curtin, Davis, Ding, Ferenczi, Fitzsimons, Greenberg, Greenberg, Gu, Guccione, Hanft, Hanft, He, Hidalgo, Hooijman, Huang, Huxley, Huxley, Ishijima, Karabina, Katz, Kentish, Korte, Levine, Mansfield, Metzger, Milani-Nejad, Morano, Morano, Moss, Muthu, Nag, Nishio, Nyitrai, Okamoto, Olsson, Pate, Patel, Podolsky, Prakash, Prakash, Pulcastro, Regnier, Regnier, Regnier, Rhodes, Sanbe, Scruggs, Sheikh, Sheikh, Sonnenblick, Stelzer, Stelzer, Stracher, Sweeney, Takagi, Toepfer, Tombe, Tombe, Ueno, Wang, Warren, Wolff, Yuan   +72 more
core   +1 more source

Erythropoietin-induced serine 727 phosphorylation of STAT3 in erythroid cells is mediated by a MEK-, ERK-, and MSK1-dependent pathway [PDF]

, 2003
Objective. Erythropoietin (EPO) is a key regulator of erythropoiesis, playing a role in both the proliferation and differentiation of erythroid cells.
Bieber, Boer, Chung, Decker, Gabrilove, Gonzalez, Goodnough, Gotoh, Haq, Jain, Jain, Jonk, Kaptein, Kirito, Kirito, Kirito, Lim, Millot, Miyazaki, Mulcahy, Ng, Schuringa, Schuringa, Schuringa, Smithgall, Socolovsky, Teglund, Tilbrook, Turkson, Watowich, Wen, Wen, Woetmann, Yokogami, Youssoufian, Yu, Zhang   +36 more
core   +1 more source

Characteristics of phosphorylated and non-phosphorylated dentine phosphoprotein [PDF]

Biochemical Journal, 1992
Heterogeneity among the odontoblast-specific, highly phosphorylated acidic protein dentine phosphoprotein (DPP) obtained from different species has been reported by several investigators. In the present study, the apparent molecular-mass variations in rabbit and mouse DPP were investigated.
M. Zeichner-David, Harold C. Slavkin, Mary MacDougall   +2 more
openaire   +3 more sources

Phospho.ELM:a database of experimentally verified phosphorylation sites in eukaryotic proteins [PDF]

, 2004
BACKGROUND: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes.
Blom, Nikolaj, Cameron, Scott, Diella, Francesca, Gemünd, Christine, Gibson, Toby J., Kuster, Bernhard, Linding, Rune, Sicheritz-Pontén, Thomas, Via, Allegra   +8 more
core   +4 more sources