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Complementary biophysical tools to investigate lipid specificity in the interaction between bioactive molecules and the plasma membrane: A review
Complementary biophysical tools to investigate lipid specificity in the interaction between bioactive molecules and the plasma membrane: A review
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Complementary biophysical tools to investigate lipid specificity in the interaction between bioactive molecules and the plasma membrane: A review

Deleu, Magali ; Crowet, Jean-Marc ; Nasir, Mehmet N. ; Lins, Laurence

Biochimica et biophysica acta, 2014-12, Vol.1838 (12), p.3171-3190 [Periódico revisado por pares]

Netherlands: Elsevier B.V

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2
Added Value of Biophysics to Study Lipid-Driven Biological Processes: The Case of Surfactins, a Class of Natural Amphiphile Molecules
Added Value of Biophysics to Study Lipid-Driven Biological Processes: The Case of Surfactins, a Class of Natural Amphiphile Molecules
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Added Value of Biophysics to Study Lipid-Driven Biological Processes: The Case of Surfactins, a Class of Natural Amphiphile Molecules

Gilliard, Guillaume ; Furlan, Aurélien L ; Smeralda, Willy ; Pršić, Jelena ; Deleu, Magali

International journal of molecular sciences, 2022-11, Vol.23 (22), p.13831 [Periódico revisado por pares]

Switzerland: MDPI AG

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3
Current developments in Coot for macromolecular model building of Electron Cryo‐microscopy and Crystallographic Data
Current developments in Coot for macromolecular model building of Electron Cryo‐microscopy and Crystallographic Data
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Current developments in Coot for macromolecular model building of Electron Cryo‐microscopy and Crystallographic Data

Casañal, Ana ; Lohkamp, Bernhard ; Emsley, Paul

Protein science, 2020-04, Vol.29 (4), p.1069-1078 [Periódico revisado por pares]

Hoboken, USA: John Wiley & Sons, Inc

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4
The mitochondria-targeted peptide SS-31 binds lipid bilayers and modulates surface electrostatics as a key component of its mechanism of action
The mitochondria-targeted peptide SS-31 binds lipid bilayers and modulates surface electrostatics as a key component of its mechanism of action
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The mitochondria-targeted peptide SS-31 binds lipid bilayers and modulates surface electrostatics as a key component of its mechanism of action

Mitchell, Wayne ; Ng, Emily A. ; Tamucci, Jeffrey D. ; Boyd, Kevin J. ; Sathappa, Murugappan ; Coscia, Adrian ; Pan, Meixia ; Han, Xianlin ; Eddy, Nicholas A. ; May, Eric R. ; Szeto, Hazel H. ; Alder, Nathan N.

The Journal of biological chemistry, 2020-05, Vol.295 (21), p.7452-7469 [Periódico revisado por pares]

United States: Elsevier Inc

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5
Polyglutamylation of tubulin's C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A
Polyglutamylation of tubulin's C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A
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Polyglutamylation of tubulin's C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A

Lessard, Dominique V. ; Zinder, Oraya J. ; Hotta, Takashi ; Verhey, Kristen J. ; Ohi, Ryoma ; Berger, Christopher L.

The Journal of biological chemistry, 2019-04, Vol.294 (16), p.6353-6363 [Periódico revisado por pares]

United States: Elsevier Inc

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6
Time-resolved serial femtosecond crystallography at the European XFEL
Time-resolved serial femtosecond crystallography at the European XFEL
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Time-resolved serial femtosecond crystallography at the European XFEL

Pandey, Suraj ; Bean, Richard ; Sato, Tokushi ; Poudyal, Ishwor ; Bielecki, Johan ; Cruz Villarreal, Jorvani ; Yefanov, Oleksandr ; Mariani, Valerio ; White, Thomas A ; Kupitz, Christopher ; Hunter, Mark ; Abdellatif, Mohamed H ; Bajt, Saša ; Bondar, Valerii ; Echelmeier, Austin ; Doppler, Diandra ; Emons, Moritz ; Frank, Matthias ; Fromme, Raimund ; Gevorkov, Yaroslav ; Giovanetti, Gabriele ; Jiang, Man ; Kim, Daihyun ; Kim, Yoonhee ; Kirkwood, Henry ; Klimovskaia, Anna ; Knoska, Juraj ; Koua, Faisal H M ; Letrun, Romain ; Lisova, Stella ; Maia, Luis ; Mazalova, Victoria ; Meza, Domingo ; Michelat, Thomas ; Ourmazd, Abbas ; Palmer, Guido ; Ramilli, Marco ; Schubert, Robin ; Schwander, Peter ; Silenzi, Alessandro ; Sztuk-Dambietz, Jolanta ; Tolstikova, Alexandra ; Chapman, Henry N ; Ros, Alexandra ; Barty, Anton ; Fromme, Petra ; Mancuso, Adrian P ; Schmidt, Marius

Nature methods, 2020-01, Vol.17 (1), p.73-78 [Periódico revisado por pares]

United States: Nature Publishing Group

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7
Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs
Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs
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Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs

Lin, Yuan ; Currie, Simon L. ; Rosen, Michael K.

The Journal of biological chemistry, 2017-11, Vol.292 (46), p.19110-19120 [Periódico revisado por pares]

United States: Elsevier Inc

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8
The Role of Capsid Maturation on Adenovirus Priming for Sequential Uncoating
The Role of Capsid Maturation on Adenovirus Priming for Sequential Uncoating
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The Role of Capsid Maturation on Adenovirus Priming for Sequential Uncoating

Pérez-Berná, Ana J. ; Ortega-Esteban, Alvaro ; Menéndez-Conejero, Rosa ; Winkler, Dennis C. ; Menéndez, Margarita ; Steven, Alasdair C. ; Flint, S.Jane ; de Pablo, Pedro J. ; San Martín, Carmen

The Journal of biological chemistry, 2012-09, Vol.287 (37), p.31582-31595 [Periódico revisado por pares]

United States: Elsevier Inc

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9
Acceleration of α-Synuclein Aggregation by Exosomes
Acceleration of α-Synuclein Aggregation by Exosomes
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Acceleration of α-Synuclein Aggregation by Exosomes

Grey, Marie ; Dunning, Christopher J. ; Gaspar, Ricardo ; Grey, Carl ; Brundin, Patrik ; Sparr, Emma ; Linse, Sara

The Journal of biological chemistry, 2015-01, Vol.290 (5), p.2969-2982 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers
Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers
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Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers

Posey, Ammon E. ; Ruff, Kiersten M. ; Harmon, Tyler S. ; Crick, Scott L. ; Li, Aimin ; Diamond, Marc I. ; Pappu, Rohit V.

The Journal of biological chemistry, 2018-03, Vol.293 (10), p.3734-3746 [Periódico revisado por pares]

United States: Elsevier Inc

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