G. Pohl

发表

Expression of human insulin-like growth factor I in bacteria: use of optimized gene fusion vectors to facilitate protein purification.

G Pohl, M. Uhlén, E. Holmgren, 1987, Biochemistry.

Plasminogen, absorbed by Escherichia coli expressing curli or by Salmonella enteritidis expressing thin aggregative fimbriae, can be activated by simultaneously captured tissue‐type plasminogen activator (t‐PA)

A. Olsén, G. Pohl, U. Sjöbring, 1994, Molecular microbiology.

Differential proteolysis and evidence for a residue exchange in tissue plasminogen activator suggest possible association between two types of protein microheterogeneity

H. Jörnvall, G. Pohl, P. Wallén, 1983, FEBS letters.

Tissue plasminogen activator: peptide analyses confirm an indirectly derived amino acid sequence, identify the active site serine residue, establish glycosylation sites, and localize variant differences.

H. Jörnvall, G. Pohl, P. Wallén, 1984, Biochemistry.

An evaluation of different enzymatic cleavage methods for recombinant fusion proteins, applied on des(1–3)insulin-like growth factor I

E. Holmgren, B. Baastrup, G. Forsberg, 1992, Journal of protein chemistry.

Binding of tissue plasminogen activator to endothelial cells. The effect on functional properties. Localization of a ligand in the B-chain of tPA.

G. Pohl, P. Wallén, O. Bäck, 1995, Thrombosis research.

Production of human tissue-type plasminogen activator in different mammalian cell lines using an Epstein-Barr virus vector.

A. Jalanko, J. Pirhonen, G. Pohl, 1990, Journal of biotechnology.

Production of a biologically active variant form of recombinant human secretin

V. Mutt, M. Uhlén, H. Jörnvall, 1988, Peptides.

Purification and characterization of a melanoma cell plasminogen activator.

H. Jörnvall, T. Ny, M. Rånby, 1983, European journal of biochemistry.

A bleeding model in rabbits demonstrate fresh clot selectivity for a genetically engineered variant of tissue-type plasminogen activator and for streptokinase.

G. Pohl, C. Mattsson, K. Wikström, 1993, Thrombosis research.

Tissue plasminogen activator mutants lacking the growth factor domain and the first kringle domain: I: DNA Constructions, Expression in Mammalian Cells, Protein Structure, Fibrin Affinity and Enzymatic Properties

Eric Nyberg, B. Löwenadler, C. Sterky, 1991 .

Tissue plasminogen activator mutants lacking the growth factor domain and the first kringle domain: II: Enzymatic properties in plasma and in vivo thrombolytic activity and clearance rates in rabbits

C. Sterky, G. Pohl, C. Mattsson, 1991 .

Human tissue-type plasminogen activator synthesized by using a baculovirus vector in insect cells compared with human plasminogen activator produced in mouse cells.

H. Steiner, M. Hellers, H. Gunne, 1988, Gene.

Sendai Virus‐Induced IFN‐α Production Analysed by Immunocytochemistry and Computerized Image Analysis

U. Andersson, T. Fehniger, J. Andersson, 1996, Scandinavian journal of immunology.

Characterization of receptors interacting specifically with the B-chain of tissue plasminogen activator on endothelial cells

G. Pohl, P. Wallén, O. Bäck, 1996 .

Pharmacokinetics and Coronary Thrombolytic Properties of Two Human Tissue‐Type Plasminogen Activator Variants Lacking the Finger‐Like, Growth Factor‐Like, and First Kringle Domains (Amino Acids 6–173) in a Canine Model

D. Collen, G. Pohl, C. Mattsson, 1990, Journal of cardiovascular pharmacology.

Sustained reflow in dogs with coronary thrombosis with K2P, a novel mutant of tissue-plasminogen activator.

W. Nichols, T. Saldeen, R. Schofield, 1992, Journal of the American College of Cardiology.

Isolation and characterization of three different carbohydrate chains from melanoma tissue plasminogen activator.

L. Kenne, G. Pohl, B. Nilsson, 1987, European journal of biochemistry.

Differences between uterine and melanoma forms of tissue plasminogen activator

H. Jörnvall, G. Pohl, P. Wallén, 1984, FEBS letters.

Proteolytically induced variations in the enzymatic properties of tissue plasminogen activator. Activations, inactivations and reactivations.

H. Jörnvall, B. Norrman, G. Pohl, 1986, European journal of biochemistry.

Porcine tissue plasminogen activator

H. Jörnvall, G. Pohl, P. Wallén, 1986, FEBS letters.

Isolation of two variants of native one‐chain tissue plasminogen activator

M. Rånby, G. Pohl, P. Wallén, 1982, FEBS letters.

Binding of tissue plasminogen activator to human endothelial cells. Importance of the B-chain as a ligand.

G. Pohl, P. Wallén, O. Bäck, 1992, The Biochemical journal.

Synergism between Tissue-Type Plasminogen Activator and a Genetically Engineered Variant Lacking the Finger Domain, the Growth Factor Domain and the First Kringle Domain

C. Sterky, G. Pohl, K. Wikström, 1991, Thrombosis and Haemostasis.

Plasminogen activator inhibitor type-1 interacts exclusively with the proteinase domain of tissue plasminogen activator.

G Pohl, M. Ericsson, P. Björquist, 1994, Biochimica et biophysica acta.

Structural characterization of tissue plasminogen activator purified by immunosorbent chromatopraphy

T. Ny, M. Rånby, G. Pohl, 1983 .