Schachman HK - Search Results

1

In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.

Zhang P, Schachman HK. Zhang P, et al. Among authors: schachman hk. Protein Sci. 1996 Jul;5(7):1290-300. doi: 10.1002/pro.5560050708. Protein Sci. 1996. PMID: 8819162 Free PMC article.

2

Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.

Peterson CB, Zhou BB, Hsieh D, Creager AN, Schachman HK. Peterson CB, et al. Among authors: schachman hk. Protein Sci. 1994 Jun;3(6):960-6. doi: 10.1002/pro.5560030611. Protein Sci. 1994. PMID: 8069225 Free PMC article.

3

Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains.

Powers VM, Yang YR, Fogli MJ, Schachman HK. Powers VM, et al. Among authors: schachman hk. Protein Sci. 1993 Jun;2(6):1001-12. doi: 10.1002/pro.5560020613. Protein Sci. 1993. PMID: 8318885 Free PMC article.

4

In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains.

Yang YR, Schachman HK. Yang YR, et al. Among authors: schachman hk. Protein Sci. 1993 Jun;2(6):1013-23. doi: 10.1002/pro.5560020614. Protein Sci. 1993. PMID: 8318886 Free PMC article.

5

Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.

Zhou BB, Schachman HK. Zhou BB, et al. Among authors: schachman hk. Protein Sci. 1993 Jan;2(1):103-12. doi: 10.1002/pro.5560020111. Protein Sci. 1993. PMID: 8443583 Free PMC article.

6

In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.

Ni X, Schachman HK. Ni X, et al. Among authors: schachman hk. Protein Sci. 2001 Mar;10(3):519-27. doi: 10.1110/ps.38901. Protein Sci. 2001. PMID: 11344320 Free PMC article.

7

Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function.

Beernink PT, Yang YR, Graf R, King DS, Shah SS, Schachman HK. Beernink PT, et al. Among authors: schachman hk. Protein Sci. 2001 Mar;10(3):528-37. doi: 10.1110/ps.39001. Protein Sci. 2001. PMID: 11344321 Free PMC article.

8

Murata LB, Schachman HK. Murata LB, et al. Among authors: schachman hk. Protein Sci. 1996 Apr;5(4):709-18. doi: 10.1002/pro.5560050416. Protein Sci. 1996. PMID: 8845761 Free PMC article.

9

A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.

Zhou BB, Waldrop GL, Lum L, Schachman HK. Zhou BB, et al. Among authors: schachman hk. Protein Sci. 1994 Jun;3(6):967-74. doi: 10.1002/pro.5560030612. Protein Sci. 1994. PMID: 8069226 Free PMC article.

10

Murata LB, Schachman HK. Murata LB, et al. Among authors: schachman hk. Protein Sci. 1996 Apr;5(4):719-28. doi: 10.1002/pro.5560050417. Protein Sci. 1996. PMID: 8845762 Free PMC article.

In our companion paper, we have shown that this putative helix is essential for OTCase folding and assembly (Murata L, Schachman HK, 1996, Protein Sci 5:709-718). Here, the similarity between OTCase and the ATCase trimer, which are 32% identical in sequence, was tes …

In our companion paper, we have shown that this putative helix is essential for OTCase folding and assembly (Murata L, Schachman H …

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