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The C-Proteinase that Processes Procollagens to Fibrillar Collagens is Identical to the Protein Previously Identified as Bone Morphogenic Protein-1

Proceedings of the National Academy of Sciences - PNAS, 1996-05, Vol.93 (10), p.5127-5130

1996

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Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process

The Journal of biological chemistry, 1987-11, Vol.262 (32), p.15696-15701

1987

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Copolymerization of pNcollagen III and collagen I. pNcollagen III decreases the rate of incorporation of collagen I into fibrils, the amount of collagen I incorporated, and the diameter of the fibrils formed

The Journal of biological chemistry, 1991-07, Vol.266 (19), p.12703-12709

1991

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Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction

Biochemical journal, 1990-06, Vol.268 (2), p.339-343

1990

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Self-assembly into fibrils of collagen II by enzymic cleavage of recombinant procollagen II. Lag period, critical concentration, and morphology of fibrils differ from collagen I

The Journal of biological chemistry, 1994-04, Vol.269 (15), p.11584-11589

1994

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Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization

The Journal of biological chemistry, 1985-12, Vol.260 (29), p.15996-16003

1985

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Cleavage of Type I Procollagen by C- and N-Proteinases Is More Rapid If the Substrate Is Aggregated with Dextran Sulfate or Polyethylene Glycol

Analytical biochemistry, 1994-12, Vol.223 (2), p.173-180

1994

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Temperature-induced post-translational over-modification of type I procollagen. Effects of over-modification of the protein on the rate of cleavage by procollagen N-proteinase and on self-assembly of collagen into fibrils

The Journal of biological chemistry, 1992-02, Vol.267 (4), p.2650-2655

1992

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Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides

The Journal of biological chemistry, 1989-07, Vol.264 (19), p.11336-11345

1989

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A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away

The Journal of biological chemistry, 1988-12, Vol.263 (35), p.19249-19255

1988

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Characterization of type I procollagen N-proteinase from fetal bovine tendon and skin. Purification of the 500-kilodalton form of the enzyme from bovine tendon

The Journal of biological chemistry, 1994-04, Vol.269 (15), p.11381-11390

1994

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Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide

Journal of molecular biology, 1989-11, Vol.210 (2), p.337-345

1989

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A substitution of cysteine for glycine 748 of the α1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away

The Journal of biological chemistry, 1988, Vol.263 (35), p.19249-19255

1988

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Polymerization of pNcollagen I and copolymerization of pNcollagen I with collagen I. A kinetic, thermodynamic, and morphologic study

The Journal of biological chemistry, 1992-11, Vol.267 (31), p.22265-22271

1992

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Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotype

The Journal of biological chemistry, 1994-04, Vol.269 (15), p.11614-11619

1994

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In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E

Blood, 1984-06, Vol.63 (6), p.1453-1459

1984

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Purification and characterization of multiple forms of human plasma prekallikrein

The Journal of biological chemistry, 1985-01, Vol.260 (1), p.400-406

1985

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Assembly of type I collagen fibrils de novo. Between 37 and 41 degrees C the process is limited by micro-unfolding of monomers

The Journal of biological chemistry, 1988-07, Vol.263 (21), p.10517-10523

1988

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Assembly of type I collagen fibrils de novo by the specific enzymic cleavage of pC collagen. The fibrils formed at about 37 degrees C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue

Annals of the New York Academy of Sciences, 1990, Vol.580, p.214-224

1990

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Direct evidence for the location of kallikrein in the striated ducts of the cat's submandibular gland by the use of specific antibody

The Journal of physiology, 1977-07, Vol.268 (3), p.793-801

1977

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Kallikrein inhibitors in rat plasma

Journal of biochemistry (Tokyo), 1977, Vol.81 (1), p.37-46

1977

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Isolation and some properties of dog and rat pancreatic kallikreins

Journal of biochemistry (Tokyo), 1977-01, Vol.81 (3), p.599-610

1977

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Purification of kallikrein from cat submaxillary gland

Advances in experimental medicine and biology, 1976, Vol.70, p.151

1976

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Enzymatic properties of human hageman factor fragment with plasma prekallikrein and synthetic substrates

Thrombosis research, 1980-05, Vol.18 (3), p.417-430

1980

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Purification of cat submaxillary kallikrein

Journal of biochemistry (Tokyo), 1979-02, Vol.85 (2), p.549-557

1979

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The C-Proteinase that Processes Procollagens to Fibrillar Collagens is Identical to the Protein Previously Identified as Bone Morphogenic Protein-1

Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process

Copolymerization of pNcollagen III and collagen I. pNcollagen III decreases the rate of incorporation of collagen I into fibrils, the amount of collagen I incorporated, and the diameter of the fibrils formed

Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction

Self-assembly into fibrils of collagen II by enzymic cleavage of recombinant procollagen II. Lag period, critical concentration, and morphology of fibrils differ from collagen I

Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization

Cleavage of Type I Procollagen by C- and N-Proteinases Is More Rapid If the Substrate Is Aggregated with Dextran Sulfate or Polyethylene Glycol

Temperature-induced post-translational over-modification of type I procollagen. Effects of over-modification of the protein on the rate of cleavage by procollagen N-proteinase and on self-assembly of collagen into fibrils

Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides

A substitution of cysteine for glycine 748 of the alpha 1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away

Characterization of type I procollagen N-proteinase from fetal bovine tendon and skin. Purification of the 500-kilodalton form of the enzyme from bovine tendon

Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide

A substitution of cysteine for glycine 748 of the α1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away

Polymerization of pNcollagen I and copolymerization of pNcollagen I with collagen I. A kinetic, thermodynamic, and morphologic study

Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotype

In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E

Purification and characterization of multiple forms of human plasma prekallikrein

Assembly of type I collagen fibrils de novo. Between 37 and 41 degrees C the process is limited by micro-unfolding of monomers

Assembly of type I collagen fibrils de novo by the specific enzymic cleavage of pC collagen. The fibrils formed at about 37 degrees C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue

Direct evidence for the location of kallikrein in the striated ducts of the cat's submandibular gland by the use of specific antibody

Kallikrein inhibitors in rat plasma

Isolation and some properties of dog and rat pancreatic kallikreins

Purification of kallikrein from cat submaxillary gland

Enzymatic properties of human hageman factor fragment with plasma prekallikrein and synthetic substrates

Purification of cat submaxillary kallikrein

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