Catalytically competent human and bovine zeta-thrombin and chimeras generated from unfolded polypeptide chains.

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Exosites in the substrate specificity of blood coagulation reactions.A control switch for prothrombinase: characterization of a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain that regulates the rate and pathway for prothrombin activation.

P2860

Q36884329-23EA1493-D4B3-443D-B796-ECB0247FD4F0 Q53595426-9F234B45-910A-4111-93CA-50E21B822265

P2860

Catalytically competent human and bovine zeta-thrombin and chimeras generated from unfolded polypeptide chains.

Item

http://www.wikidata.org/entity/Q42842088

description

1992 nî lūn-bûn

@nan

1992年の論文

@ja

1992年論文

@yue

1992年論文

@zh-hant

1992年論文

@zh-hk

1992年論文

@zh-mo

1992年論文

@zh-tw

1992年论文

@wuu

1992年论文

@zh

1992年论文

@zh-cn

name

Catalytically competent human ...... m unfolded polypeptide chains.

@en

Catalytically competent human ...... m unfolded polypeptide chains.

@nl

type

Item

label

Catalytically competent human ...... m unfolded polypeptide chains.

@en

Catalytically competent human ...... m unfolded polypeptide chains.

@nl

prefLabel

Catalytically competent human ...... m unfolded polypeptide chains.

@en

Catalytically competent human ...... m unfolded polypeptide chains.

@nl

P1476

Catalytically competent human ...... m unfolded polypeptide chains.

@en

P2093

D V Brezniak

http://www.w3.org/2001/XMLSchema#string

J A Shafer

http://www.w3.org/2001/XMLSchema#string

J W Fenton

http://www.w3.org/2001/XMLSchema#string

S D Lewis

http://www.w3.org/2001/XMLSchema#string

P2860

Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin

The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell

Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization

Cofactor proteins in the assembly and expression of blood clotting enzyme complexes

Determination of the operational molarity of solutions of bovine alpha-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorimetric titration

Primary structure of human prethrombin 2 and alpha-thrombin

Spectroscopic determination of tryptophan and tyrosine in proteins

Solubility as a function of protein structure and solvent components.

Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins.

DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS.

P304

998-1006

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P31

scholarly article

P356

10.1002/PRO.5560010805

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

1992-08-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

21852092

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P698

1304387

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P932

2142167

http://www.w3.org/2001/XMLSchema#string

Catalytically competent human and bovine zeta-thrombin and chimeras generated from unfolded polypeptide chains.

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P2860

P2860

Catalytically competent human and bovine zeta-thrombin and chimeras generated from unfolded polypeptide chains.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932