Photoaffinity Labeling of the Human Receptor for Urokinase-Type Plasminogen Activator Using a Decapeptide Antagonist. Evidence for a Composite Ligand-Binding Site and a Short Interdomain Separation†

Michael Ploug; Søren Østergaard; Lars Bo Laurenborg Hansen; Arne Holm; Keld Danø

doi:10.1021/bi972787k

Photoaffinity Labeling of the Human Receptor for Urokinase-Type Plasminogen Activator Using a Decapeptide Antagonist. Evidence for a Composite Ligand-Binding Site and a Short Interdomain Separation†

Biochemistry ◽

10.1021/bi972787k ◽

1998 ◽

Vol 37 (11) ◽

pp. 3612-3622 ◽

Cited By ~ 51

Author(s):

Michael Ploug ◽

Søren Østergaard ◽

Lars Bo Laurenborg Hansen ◽

Arne Holm ◽

Keld Danø

Keyword(s):

Ligand Binding ◽

Binding Site ◽

Plasminogen Activator ◽

Photoaffinity Labeling ◽

Ligand Binding Site ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator ◽

Human Receptor

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Identification of Specific Sites Involved in Ligand Binding by Photoaffinity Labeling of the Receptor for the Urokinase-Type Plasminogen Activator. Residues Located at Equivalent Positions in uPAR Domains I and III Participate in the Assembly of a Composite Ligand-Binding Site†

Biochemistry ◽

10.1021/bi981203r ◽

1998 ◽

Vol 37 (47) ◽

pp. 16494-16505 ◽

Cited By ~ 36

Author(s):

Michael Ploug

Keyword(s):

Ligand Binding ◽

Binding Site ◽

Plasminogen Activator ◽

Photoaffinity Labeling ◽

Ligand Binding Site ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator

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Intrinsic photoaffinity labeling of the cholecystokinin receptor provides dual constraints for modeling the ligand-binding site

Gastroenterology ◽

10.1016/s0016-5085(98)81885-4 ◽

1998 ◽

Vol 114 ◽

pp. A466

Author(s):

E.M. Hadac ◽

D.I. Pinon ◽

Z. Ji ◽

E.L. Holicky ◽

T. Lybrand ◽

...

Keyword(s):

Ligand Binding ◽

Binding Site ◽

Photoaffinity Labeling ◽

Ligand Binding Site ◽

Cholecystokinin Receptor ◽

Dual Constraints

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Direct Photoaffinity Labeling of Cellular Retinoic Acid-Binding Protein I (CRABP-I) withall-trans-Retinoic Acid: Identification of Amino Acids in the Ligand Binding Site†

Biochemistry ◽

10.1021/bi000321n ◽

2000 ◽

Vol 39 (41) ◽

pp. 12568-12574 ◽

Cited By ~ 12

Author(s):

Guangping Chen ◽

Anna Radominska-Pandya

Keyword(s):

Amino Acids ◽

Retinoic Acid ◽

Ligand Binding ◽

Binding Site ◽

Binding Protein ◽

Photoaffinity Labeling ◽

Ligand Binding Site ◽

Acid Binding Protein ◽

Trans Retinoic Acid ◽

Crabp I

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Ligand interaction between urokinase-type plasminogen activator and its receptor probed with 8-anilino-1-naphthalene sulphonate: Evidence for a hydrophobic binding site exposed only on the intact receptor

Fibrinolysis and Proteolysis ◽

10.1016/0268-9499(94)90309-3 ◽

1994 ◽

Vol 8 ◽

pp. 9

Author(s):

Michael Ploug ◽

Vincent Ellis ◽

Keld Dane

Keyword(s):

Binding Site ◽

Plasminogen Activator ◽

Ligand Interaction ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator ◽

Hydrophobic Binding

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Down-regulation of integrin αMβ2 ligand-binding function by the urokinase-type plasminogen activator receptor

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2006.07.179 ◽

2006 ◽

Vol 348 (3) ◽

pp. 1184-1193 ◽

Cited By ~ 8

Author(s):

Man-Li Tang ◽

Le-Sheng Kong ◽

S.K. Alex Law ◽

Suet-Mien Tan

Keyword(s):

Ligand Binding ◽

Plasminogen Activator ◽

Down Regulation ◽

Binding Function ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator ◽

Plasminogen Activator Receptor

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Ligand Interaction between Urokinase-Type Plasminogen Activator and Its Receptor Probed with 8-Anilino-1-naphthalenesulfonate. Evidence for a Hydrophobic Binding Site Exposed Only on the Intact Receptor

Biochemistry ◽

10.1021/bi00196a017 ◽

1994 ◽

Vol 33 (30) ◽

pp. 8991-8997 ◽

Cited By ~ 72

Author(s):

Michael Ploug ◽

Vincent Ellis ◽

Keld Danoe

Keyword(s):

Binding Site ◽

Plasminogen Activator ◽

Ligand Interaction ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator ◽

Hydrophobic Binding

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Quantitative assessment of interaction of urokinase-type plasminogen activator and its receptor (CD87) by use of a solid-phase uPA-ligand binding assay

Fibrinolysis and Proteolysis ◽

10.1016/s0268-9499(97)80004-5 ◽

1997 ◽

Vol 11 (1) ◽

pp. 11-19 ◽

Cited By ~ 7

Author(s):

L. Goretzki ◽

J. Bognacki ◽

M. Koppitz ◽

P. Rettenberger ◽

V. Magdolen ◽

...

Keyword(s):

Ligand Binding ◽

Plasminogen Activator ◽

Quantitative Assessment ◽

Binding Assay ◽

Solid Phase ◽

Ligand Binding Assay ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator

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Avian urokinase-type plasminogen activator (u-PA) lacks the putative binding site for plasminogen activator inhibitor (PAI) and is resistant to inhibition by human PAI-1 and PAI-2

Fibrinolysis and Proteolysis ◽

10.1016/s0268-9499(95)80070-0 ◽

1995 ◽

Vol 9 (2) ◽

pp. 93-99 ◽

Cited By ~ 3

Author(s):

J.E. Testa ◽

S. Stefansson ◽

T. Sioussat ◽

J.P. Quigley

Keyword(s):

Binding Site ◽

Plasminogen Activator ◽

Plasminogen Activator Inhibitor ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator ◽

Putative Binding Site ◽

Activator Inhibitor ◽

Pai 1

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Mapping Part of the Functional Epitope for Ligand Binding on the Receptor for Urokinase-type Plasminogen Activator by Site-directed Mutagenesis

Journal of Biological Chemistry ◽

10.1074/jbc.274.53.37995 ◽

1999 ◽

Vol 274 (53) ◽

pp. 37995-38003 ◽

Cited By ~ 57

Author(s):

Henrik Gårdsvoll ◽

Keld Danø ◽

Michael Ploug

Keyword(s):

Ligand Binding ◽

Plasminogen Activator ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator

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Ligand Binding Regions in the Receptor for Urokinase-type Plasminogen Activator

Journal of Biological Chemistry ◽

10.1074/jbc.m011347200 ◽

2001 ◽

Vol 276 (31) ◽

pp. 28946-28953 ◽

Cited By ~ 8

Author(s):

Olin D. Liang ◽

Triantafyllos Chavakis ◽

Sandip M. Kanse ◽

Klaus T. Preissner

Keyword(s):

Ligand Binding ◽

Plasminogen Activator ◽

Type Plasminogen Activator ◽

Urokinase Type Plasminogen Activator ◽

Binding Regions

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