Identification of VEGFR2 as the Histatin-1 receptor in endothelial cells.

[1]  Xiaobing Fu,et al.  Histatin 1 enhanced the speed and quality of wound healing through regulating the behaviour of fibroblast , 2021, Cell proliferation.

[2]  T. Frączyk.  Phosphorylation Impacts Cu(II) Binding by ATCUN Motifs , 2021, Inorganic chemistry.

[3]  Gang Wu,et al.  Human Salivary Histatin-1-Functionalized Gelatin Methacrylate Hydrogels Promote the Regeneration of Cartilage and Subchondral Bone in Temporomandibular Joints , 2021, Pharmaceuticals.

[4]  A. Criollo,et al.  Histatin‐1 is a novel osteogenic factor that promotes bone cell adhesion, migration, and differentiation , 2021, Journal of tissue engineering and regenerative medicine.

[5]  Qiong Gao,et al.  Effects and mechanisms of histatins as novel skin wound-healing agents. , 2021, Journal of tissue viability.

[6]  G. Simone,et al.  Molecular Bases of VEGFR-2-Mediated Physiological Function and Pathological Role , 2020, Frontiers in Cell and Developmental Biology.

[7]  D. Ma,et al.  Human Salivary Histatin-1 Promotes Osteogenic Cell Spreading on Both Bio-Inert Substrates and Titanium SLA Surfaces , 2020, Frontiers in Bioengineering and Biotechnology.

[8]  F. Bikker,et al.  Human Salivary Histatin-1 Is More Efficacious in Promoting Acute Skin Wound Healing Than Acellular Dermal Matrix Paste , 2020, Frontiers in Bioengineering and Biotechnology.

[9]  L. Bian,et al.  Injectable supramolecular gelatin hydrogel loading of resveratrol and histatin-1 for burn wound therapy. , 2020, Biomaterials science.

[10]  E. Morselli,et al.  PKD2/polycystin-2 induces autophagy by forming a complex with BECN1 , 2020, Autophagy.

[11]  Gang Wu,et al.  Human salivary histatin‐1 (Hst1) promotes bone morphogenetic protein 2 (BMP2)‐induced osteogenesis and angiogenesis , 2020, FEBS open bio.

[12]  Jing Wang,et al.  Histatin1-modified thiolated chitosan hydrogels enhance wound healing by accelerating cell adhesion, migration and angiogenesis. , 2020, Carbohydrate polymers.

[13]  V. Torres,et al.  Focal adhesion kinase–dependent activation of the early endocytic protein Rab5 is associated with cell migration , 2019, The Journal of Biological Chemistry.

[14]  V. Torres,et al.  Histatin-1 counteracts the cytotoxic and antimigratory effects of zoledronic acid in endothelial and osteoblast-like cells. , 2019, Journal of periodontology.

[15]  K. Hristova,et al.  Direct measurements of VEGF–VEGFR2 binding affinities reveal the coupling between ligand binding and receptor dimerization , 2019, The Journal of Biological Chemistry.

[16]  V. Torres,et al.  Histatins, wound healing, and cell migration. , 2018, Oral diseases.

[17]  E. Veerman,et al.  Salivary peptide histatin 1 mediated cell adhesion: a possible role in mesenchymal-epithelial transition and in pathologies , 2018, Biological chemistry.

[18]  Torsten Schwede,et al.  SWISS-MODEL: homology modelling of protein structures and complexes , 2018, Nucleic Acids Res..

[19]  L. Leyton,et al.  Single-molecule measurements of the effect of force on Thy-1/αvβ3-integrin interaction using nonpurified proteins , 2017, Molecular biology of the cell.

[20]  Kathryn L Haas,et al.  Specific Histidine Residues Confer Histatin Peptides with Copper-Dependent Activity against Candida albicans. , 2017, Biochemistry.

[21]  V. Palma,et al.  The salivary peptide histatin‐1 promotes endothelial cell adhesion, migration, and angiogenesis , 2017, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[22]  R. Hoebe,et al.  Human salivary peptide histatin‐1 stimulates epithelial and endothelial cell adhesion and barrier function , 2017, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[23]  Rajesh Raju,et al.  VEGF-A/VEGFR2 signaling network in endothelial cells relevant to angiogenesis , 2016, Journal of Cell Communication and Signaling.

[24]  Muhammad Sohail Zafar,et al.  Histatin peptides: Pharmacological functions and their applications in dentistry , 2016, Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society.

[25]  A. Roitberg,et al.  Long-Time-Step Molecular Dynamics through Hydrogen Mass Repartitioning. , 2015, Journal of chemical theory and computation.

[26]  M. Allende,et al.  Independent Anti‐Angiogenic Capacities of Coagulation Factors X and Xa , 2014, Journal of cellular physiology.

[27]  P. di Nardo,et al.  Histatins: salivary peptides with copper(II)‐ and zinc(II)‐binding motifs , 2014, The FEBS journal.

[28]  T. Crombleholme,et al.  Role of salivary vascular endothelial growth factor (VEGF) in palatal mucosal wound healing , 2013, Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society.

[29]  Zhanglin Lin,et al.  Facile expression and purification of the antimicrobial peptide histatin 1 with a cleavable self-aggregating tag (cSAT) in Escherichia coli. , 2013, Protein expression and purification.

[30]  S. Koch,et al.  Signal transduction by vascular endothelial growth factor receptors. , 2012, Cold Spring Harbor perspectives in medicine.

[31]  F. Winkler,et al.  Thermodynamic and structural description of allosterically regulated VEGFR-2 dimerization. , 2012, Blood.

[32]  Ora Schueler-Furman,et al.  Rosetta FlexPepDock web server—high resolution modeling of peptide–protein interactions , 2011, Nucleic Acids Res..

[33]  Nir London,et al.  Sub‐angstrom modeling of complexes between flexible peptides and globular proteins , 2010, Proteins.

[34]  S. Gibbs,et al.  Structure‐activity analysis of histatin, a potent wound healing peptide from human saliva: cyclization of histatin potentiates molar activity 1000‐fold , 2009, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[35]  S. Gibbs,et al.  Histatins Enhance Wound Closure with Oral and Non-oral Cells , 2009, Journal of dental research.

[36]  E. Veerman,et al.  Histatins are the major wound‐closure stimulating factors in human saliva as identified in a cell culture assay , 2008, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[37]  G. Hummer,et al.  Theory, analysis, and interpretation of single-molecule force spectroscopy experiments , 2008, Proceedings of the National Academy of Sciences.

[38]  Taehoon Kim,et al.  CHARMM‐GUI: A web‐based graphical user interface for CHARMM , 2008, J. Comput. Chem..

[39]  Yan Liu,et al.  Transactivation of vascular endothelial growth factor receptor-2 by interleukin-8 (IL-8/CXCL8) is required for IL-8/CXCL8-induced endothelial permeability. , 2007, Molecular biology of the cell.

[40]  J. Gratton,et al.  Phosphorylation of Tyrosine 801 of Vascular Endothelial Growth Factor Receptor-2 Is Necessary for Akt-dependent Endothelial Nitric-oxide Synthase Activation and Nitric Oxide Release from Endothelial Cells* , 2007, Journal of Biological Chemistry.

[41]  Holger Gohlke,et al.  The Amber biomolecular simulation programs , 2005, J. Comput. Chem..

[42]  David Baker,et al.  Protein structure prediction and analysis using the Robetta server , 2004, Nucleic Acids Res..

[43]  W. Min,et al.  Etk/Bmx Transactivates Vascular Endothelial Growth Factor 2 and Recruits Phosphatidylinositol 3-Kinase to Mediate the Tumor Necrosis Factor-induced Angiogenic Pathway* , 2003, Journal of Biological Chemistry.

[44]  K Schulten,et al.  VMD: visual molecular dynamics. , 1996, Journal of molecular graphics.

[45]  R. Raines,et al.  Analysis of Receptor-Ligand Interactions. , 1995, Journal of chemical education.

[46]  Carlos Bustamante,et al.  Optical-trap force transducer that operates by direct measurement of light momentum. , 2003, Methods in enzymology.