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Site-specific N-glycolylation profiles in a5b1 integrin from rat liver

ABSTRACT: To visualize glycosylation in the context of the integrin structure, the quantitative site-specific glycosylation profiles of a5b1 integrin were determined and the main representative glycans were mapped onto a homology model of rat a5b1 integrin in its bent-closed inactive conformation.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive HF

ORGANISM(S): Rattus Norvegicus (rat) Homo Sapiens (human)

TISSUE(S): Liver

SUBMITTER: Proteomics Core Facility

LAB HEAD: Ekaterina Mirgorodskaya

PROVIDER: PXD031334 | Pride | 2024-07-25

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	2942-2_ChT-G_5-30_acNeuAc_PrecQuant_QEHF_190815_48.msf	Msf
	2942-2_ChT-G_5-30_acNeuAc_PrecQuant_QEHF_190815_48.pdResult	Other
	2942-2_G_AspN-ns_5-30_acNeuAc_PrecQuant_QEHF_190402_12.msf	Msf
	2942-2_G_AspN-ns_5-30_acNeuAc_PrecQuant_QEHF_190402_12.pdResult	Other
	2942-2_G_GluC-ns_5-30_acNeuAc_PrecQuant_QEHF_190402_12.msf	Msf

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