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Tunable Membrane Binding of the Intrinsically Disordered Dehydrin Lti30, a Cold-Induced Plant Stress Protein

The Plant cell, 2011-06, Vol.23 (6), p.2391-2404

2011

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The plant dehydrin Lti30 stabilizes lipid lamellar structures in varying hydration conditions[S]

Journal of lipid research, 2020-07, Vol.61 (7), p.1014-1024

2020

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Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse

Plant physiology (Bethesda), 2008-12, Vol.148 (4), p.1925-1937

2008

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Membrane-Induced Folding of the Plant Stress Dehydrin Lti30

Plant physiology (Bethesda), 2016-06, Vol.171 (2), p.932-943

2016

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The disordered plant dehydrin Lti30 protects the membrane during water-related stress by cross-linking lipids

The Journal of biological chemistry, 2019-04, Vol.294 (16), p.6468-6482

2019

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Structural Investigation of Disordered Stress Proteins. Comparison of Full-Length Dehydrins with Isolated Peptides of Their Conserved Segments

Plant physiology (Bethesda), 2006-06, Vol.141 (2), p.638-650

2006

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Membrane-induced folding of the plant-stress protein Lti30

Plant physiology (Bethesda), 2016-04, p.pp.01531.2015

2016

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Membrane-Induced Folding of the Plant Stress Dehydrin Lti301[OPEN]

Plant physiology (Bethesda), 2016-04, Vol.171 (2), p.932-943

2016

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lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation

Journal of experimental botany, 2012-08, Vol.63 (13), p.4919-4929

2012

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The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 fromCraterostigma plantagineumis responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation

Journal of experimental botany, 2012-01, Vol.63 (13), p.4919-4929

2012

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Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse1[W]

Plant physiology (Bethesda), 2008-12, Vol.148 (4), p.1925-1937

2008

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Structural Investigation of Disordered Stress Proteins. Comparison of Full-Length Dehydrins with Isolated Peptides of Their Conserved Segments1

Plant physiology (Bethesda), 2006-06, Vol.141 (2), p.638-650

2006

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A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase

Acta crystallographica. Section D, Biological crystallography., 2002-04, Vol.58 (4), p.591-600

2002

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Cell-free transfer of phosphatidylinositol between membrane fractions isolated from soybean

Plant physiology (Bethesda), 1996-02, Vol.110 (2), p.631-637

1996

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The effects of a non-specific lipid transfer protein on a cell-free reconstitution of phosphatidylinositol transfer to plant plasma membranes

Plant science (Limerick), 1994, Vol.99 (1), p.55-62

1994

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Tunable Membrane Binding of the Intrinsically Disordered Dehydrin Lti30, a Cold-Induced Plant Stress Protein

The plant dehydrin Lti30 stabilizes lipid lamellar structures in varying hydration conditions[S]

Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse

Membrane-Induced Folding of the Plant Stress Dehydrin Lti30

The disordered plant dehydrin Lti30 protects the membrane during water-related stress by cross-linking lipids

Structural Investigation of Disordered Stress Proteins. Comparison of Full-Length Dehydrins with Isolated Peptides of Their Conserved Segments

Membrane-induced folding of the plant-stress protein Lti30

Membrane-Induced Folding of the Plant Stress Dehydrin Lti301[OPEN]

lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation

The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 fromCraterostigma plantagineumis responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation

Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse1[W]

Structural Investigation of Disordered Stress Proteins. Comparison of Full-Length Dehydrins with Isolated Peptides of Their Conserved Segments1

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase

Cell-free transfer of phosphatidylinositol between membrane fractions isolated from soybean

The effects of a non-specific lipid transfer protein on a cell-free reconstitution of phosphatidylinositol transfer to plant plasma membranes

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