[HTML][HTML] Two non-proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS letters, 1998 - Elsevier
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(Rfree= 23.6%) for all data between 40.0 and …

[引用][C] Two non‐proline cis peptide bonds may be important for factor XIII function

MS Weiss - FEBS Lett, 1998 - cir.nii.ac.jp
Two non‐proline cis peptide bonds may be important for factor XIII function | CiNii Research
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[PDF][PDF] Two non-proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - structure - core.ac.uk
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(Rfree= 23.6%) for all data between 40.0 and …

Two non-proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS letters, 1998 - pubmed.ncbi.nlm.nih.gov
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(Rfree= 23.6%) for all data between 40.0 and …

Two non-proline cis peptide bonds may be important for factor XIII function.

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS Letters, 1998 - europepmc.org
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(Rfree= 23.6%) for all data between 40.0 and …

Two non‐proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS Letters, 1998 - Wiley Online Library
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R‐factor of 18.3%(R free= 23.6%) for all data between 40.0 …

Two non-proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS Letters, 1998 - elibrary.ru
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(R free= 23.6%) for all data between 40.0 …

Two non-proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS Letters, 1998 - infona.pl
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(R free= 23.6%) for all data between 40.0 …

Two non-proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS Letters, 1998 - ui.adsabs.harvard.edu
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(R free= 23.6%) for all data between 40.0 …

Two non-proline cis peptide bonds may be important for factor XIII function

MS Weiss, HJ Metzner, R Hilgenfeld - FEBS Letters, 1998 - research.uni-luebeck.de
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic
crystal form and refined to an R-factor of 18.3%(R (free)= 23.6%) for all data between 40.0 …