R W Carrell|A M Lesk - JoVE Visualize

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Proceedings of the National Academy of Sciences of the United States of America|January 5, 2000

Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational diseaseB Gooptu, B Hazes, W S Chang, et al.

Hemoglobin|January 1, 1980

Hemoglobin Volga, beta 27 (B9) Ala replaced by Asp: functional and clinical correlations of an unstable hemoglobinP A Ockelford, A Y Liang, R M Wells, et al.

FEBS Letters|July 22, 1991

Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpinsD J Perry, M Daly, P L Harper, et al.

Journal of Biomolecular NMR|December 22, 1999

Tendamistat surface accessibility to the TEMPOL paramagnetic probeM Scarselli, A Bernini, C Segoni, et al.

Science (New York, N.Y.)|August 15, 1986

The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structureC Chothia, A M Lesk, M Levitt, et al.

Journal of Thrombosis and Haemostasis : JTH|May 14, 2004

Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosisJ Corral, J A Huntington, R González-Conejero, et al.

Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis|February 1, 1995

Two novel antithrombin variants, Asn187Asp and Asn187Lys, indicate a functional role for asparagine 187D J Perry, C Marshall, J Y Borg, et al.

Journal of Molecular Biology|October 5, 1992

Structural repertoire of the human VH segmentsC Chothia, A M Lesk, E Gherardi, et al.

Nature|July 22, 1982

Structure and variation of human alpha 1-antitrypsinR W Carrell, J O Jeppsson, C B Laurell, et al.

British Journal of Haematology|March 1, 1991

The incidence of dysfunctional antithrombin variants: four cases in 210 patients with thromboembolic diseaseP L Harper, R J Luddington, M Daly, et al.

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Showing results (181-190 of 204) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|January 5, 2000

Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational diseaseB Gooptu, B Hazes, W S Chang, et al.

Hemoglobin|January 1, 1980

Hemoglobin Volga, beta 27 (B9) Ala replaced by Asp: functional and clinical correlations of an unstable hemoglobinP A Ockelford, A Y Liang, R M Wells, et al.

FEBS Letters|July 22, 1991

Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpinsD J Perry, M Daly, P L Harper, et al.

Journal of Biomolecular NMR|December 22, 1999

Tendamistat surface accessibility to the TEMPOL paramagnetic probeM Scarselli, A Bernini, C Segoni, et al.

Science (New York, N.Y.)|August 15, 1986

The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structureC Chothia, A M Lesk, M Levitt, et al.

Journal of Thrombosis and Haemostasis : JTH|May 14, 2004

Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosisJ Corral, J A Huntington, R González-Conejero, et al.

Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis|February 1, 1995

Two novel antithrombin variants, Asn187Asp and Asn187Lys, indicate a functional role for asparagine 187D J Perry, C Marshall, J Y Borg, et al.

Journal of Molecular Biology|October 5, 1992

Structural repertoire of the human VH segmentsC Chothia, A M Lesk, E Gherardi, et al.

Nature|July 22, 1982

Structure and variation of human alpha 1-antitrypsinR W Carrell, J O Jeppsson, C B Laurell, et al.

British Journal of Haematology|March 1, 1991

The incidence of dysfunctional antithrombin variants: four cases in 210 patients with thromboembolic diseaseP L Harper, R J Luddington, M Daly, et al.

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