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Having thrived in Eurasia for 350,000 years Neandertals disappeared from the record around 40,000–37,000 years ago, after modern humans entered Europe. It was a complex process of population interactions that included cultural exchanges and admixture between Neandertals and dispersing groups of modern humans. In Europe Neandertals are always associated with the Mousterian while the Aurignacian is associated with modern humans only. The onset of the Aurignacian is preceded by “transitional” industries which show some similarities with the Mousterian but also contain modern tool forms. Information on these industries is often incomplete or disputed and this is true of the Uluzzian. We present the results of taphonomic, typological and technological analyses of two Uluzzian sites, Grotta La Fabbrica (Tuscany) and the newly discovered site of Colle Rotondo (Latium). Comparisons with Castelcivita and Grotta del Cavallo show that the Uluzzian is a coherent cultural unit lasting about five millennia, replaced by the Protoaurignacian before the eruption of the Campanian Ignimbrite. The lack of skeletal remains at our two sites and the controversy surrounding the stratigraphic position of modern human teeth at Cavallo makes it difficult to reach agreement about authorship of the Uluzzian, for which alternative hypotheses have been proposed. Pending the discovery of DNA or further human remains, these hypotheses can only be evaluated by archaeological arguments, i.e. evidence of continuities and discontinuities between the Uluzzian and the preceding and succeeding culture units in Italy. However, in the context of “transitional” industries with disputed dates for the arrival of modern humans in Europe, and considering the case of the Châtelperronian, an Upper Paleolithic industry made by Neandertals, typo-technology used as an indicator of hominin authorship has limited predictive value. We corroborate previous suggestions that the Middle-to-Upper Paleolithic transition occur

Having thrived in Eurasia for 350,000 years Neandertals disappeared from the record around 40,000–37,000 years ago, after modern humans entered Europe. It was a complex process of population interactions that included cultural exchanges and admixture between Neandertals and dispersing groups of modern humans. In Europe Neandertals are always associated with the Mousterian while the Aurignacian is associated with modern humans only. The onset of the Aurignacian is preceded by “transitional” industries which show some similarities with the Mousterian but also contain modern tool forms. Information on these industries is often incomplete or disputed and this is true of the Uluzzian. We present the results of taphonomic, typological and technological analyses of two Uluzzian sites, Grotta La Fabbrica (Tuscany) and the newly discovered site of Colle Rotondo (Latium). Comparisons with Castelcivita and Grotta del Cavallo show that the Uluzzian is a coherent cultural unit lasting about five millennia, replaced by the Protoaurignacian before the eruption of the Campanian Ignimbrite. The lack of skeletal remains at our two sites and the controversy surrounding the stratigraphic position of modern human teeth at Cavallo makes it difficult to reach agreement about authorship of the Uluzzian, for which alternative hypotheses have been proposed. Pending the discovery of DNA or further human remains, these hypotheses can only be evaluated by archaeological arguments, i.e. evidence of continuities and discontinuities between the Uluzzian and the preceding and succeeding culture units in Italy. However, in the context of “transitional” industries with disputed dates for the arrival of modern humans in Europe, and considering the case of the Châtelperronian, an Upper Paleolithic industry made by Neandertals, typo-technology used as an indicator of hominin authorship has limited predictive value. We corroborate previous suggestions that the Middle-to-Upper Paleolithic transition occu

Contains fulltext : 128336.pdf (publisher's version ) (Open Access)

Contains fulltext : 128336.pdf (publisher's version ) (Open Access)

Contains fulltext : 128336.pdf (publisher's version ) (Open Access)

Item does not contain fulltext, We report the fabrication of a patterned protein array using three orthogonal methods of immobilization that are detected exploiting a fluorogenic surface. Upon reaction of thiols, the fluorogenic tether reports the bond formation by an instantaneous rise in (blue) fluorescence intensity providing a means to visualize the immobilization even of nonfluorescent biomolecules. First, the covalent, oriented immobilization of a visible fluorescent protein (TFP) modified to display a single cysteine residue was detected. Colocalization of the fluorescence of the immobilized TFP and the fluorogenic group provided a direct tool to distinguish covalent bond formation from physisorption of proteins. Subsequent orthogonal immobilization of thiol-functionalized biomolecules could be conveniently detected by fluorescence microscopy using the fluorogenic surface. A thiol-modified nitrilotriacetate ligand was immobilized for binding of hexahistidine-tagged red-fluorescing TagRFP, while an appropriately modified biotin was immobilized for binding of Cy5-labeled streptavidin.

Item does not contain fulltext, We report the fabrication of a patterned protein array using three orthogonal methods of immobilization that are detected exploiting a fluorogenic surface. Upon reaction of thiols, the fluorogenic tether reports the bond formation by an instantaneous rise in (blue) fluorescence intensity providing a means to visualize the immobilization even of nonfluorescent biomolecules. First, the covalent, oriented immobilization of a visible fluorescent protein (TFP) modified to display a single cysteine residue was detected. Colocalization of the fluorescence of the immobilized TFP and the fluorogenic group provided a direct tool to distinguish covalent bond formation from physisorption of proteins. Subsequent orthogonal immobilization of thiol-functionalized biomolecules could be conveniently detected by fluorescence microscopy using the fluorogenic surface. A thiol-modified nitrilotriacetate ligand was immobilized for binding of hexahistidine-tagged red-fluorescing TagRFP, while an appropriately modified biotin was immobilized for binding of Cy5-labeled streptavidin.

Item does not contain fulltext, We report the fabrication of a patterned protein array using three orthogonal methods of immobilization that are detected exploiting a fluorogenic surface. Upon reaction of thiols, the fluorogenic tether reports the bond formation by an instantaneous rise in (blue) fluorescence intensity providing a means to visualize the immobilization even of nonfluorescent biomolecules. First, the covalent, oriented immobilization of a visible fluorescent protein (TFP) modified to display a single cysteine residue was detected. Colocalization of the fluorescence of the immobilized TFP and the fluorogenic group provided a direct tool to distinguish covalent bond formation from physisorption of proteins. Subsequent orthogonal immobilization of thiol-functionalized biomolecules could be conveniently detected by fluorescence microscopy using the fluorogenic surface. A thiol-modified nitrilotriacetate ligand was immobilized for binding of hexahistidine-tagged red-fluorescing TagRFP, while an appropriately modified biotin was immobilized for binding of Cy5-labeled streptavidin.