[HTML][HTML] ICln159 Folds into a Pleckstrin Homology Domain-like Structure: INTERACTION WITH KINASES AND THE SPLICING FACTOR LSm4*[boxs]
J Furst, A Schedlbauer, R Gandini… - Journal of Biological …, 2005 - ASBMB
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
[PDF][PDF] ICln159 Folds into a Pleckstrin Homology Domain-like Structure
J Furst, A Schedlbauer, R Gandini, ML Garavaglia… - 2005 - researchgate.net
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
[HTML][HTML] ICln159 Folds into a Pleckstrin Homology Domain-like Structure: INTERACTION WITH KINASES AND THE SPLICING FACTOR LSm4
J Fürst, A Schedlbauer, R Gandini… - Journal of Biological …, 2005 - Elsevier
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ICln (159) folds into a pleckstrin homology domain-like structure
J Furst, A Schedlbauer, R Gandini… - THE JOURNAL OF …, 2005 - air.unimi.it
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4
J Fürst, A Schedlbauer, R Gandini… - The Journal of …, 2005 - pubmed.ncbi.nlm.nih.gov
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
[PDF][PDF] ICln159 Folds into a Pleckstrin Homology Domain-like Structure
J Furst, A Schedlbauer, R Gandini, ML Garavaglia… - 2005 - academia.edu
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4.
J Fürst, A Schedlbauer, R Gandini… - The Journal of …, 2005 - europepmc.org
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ICln159 folds into a pleckstrin homology domain-like structure: Interaction with kinases and the splicing factor LSm4
A Fürst, A Schedlbauer, R Gandini… - Journal of Biological …, 2005 - repub.eur.nl
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
[PDF][PDF] ICln159 Folds into a Pleckstrin Homology Domain-like Structure
J Furst, A Schedlbauer, R Gandini, ML Garavaglia… - 2005 - academia.edu
ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …
ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume …