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Synthetic Biology UK 2015

Biochem Soc Trans (2016) 44 (3): 675–677.
Biochem Soc Trans (2016) 44 (3): 678–680.
Biochem Soc Trans (2016) 44 (3): 681–683.
Biochem Soc Trans (2016) 44 (3): 684–686.
Biochem Soc Trans (2016) 44 (3): 687–688.
Biochem Soc Trans (2016) 44 (3): 689–691.
Biochem Soc Trans (2016) 44 (3): 692–695.
Biochem Soc Trans (2016) 44 (3): 696–701.
Biochem Soc Trans (2016) 44 (3): 702–708.
Biochem Soc Trans (2016) 44 (3): 709–715.
Biochem Soc Trans (2016) 44 (3): 716–722.
Biochem Soc Trans (2016) 44 (3): 723–730.
Biochem Soc Trans (2016) 44 (3): 731–737.
Biochem Soc Trans (2016) 44 (3): 738–744.

Membrane Proteins From A to Z

Biochem Soc Trans (2016) 44 (3): 745–752.
Biochem Soc Trans (2016) 44 (3): 753–759.
Biochem Soc Trans (2016) 44 (3): 760–765.
Biochem Soc Trans (2016) 44 (3): 766–773.
Biochem Soc Trans (2016) 44 (3): 774–782.
Biochem Soc Trans (2016) 44 (3): 783–789.
Biochem Soc Trans (2016) 44 (3): 790–795.
Biochem Soc Trans (2016) 44 (3): 796–801.
Biochem Soc Trans (2016) 44 (3): 802–809.
Biochem Soc Trans (2016) 44 (3): 810–823.
Biochem Soc Trans (2016) 44 (3): 824–830.
Biochem Soc Trans (2016) 44 (3): 831–837.
Biochem Soc Trans (2016) 44 (3): 838–844.
Biochem Soc Trans (2016) 44 (3): 845–850.
Biochem Soc Trans (2016) 44 (3): 851–855.
Biochem Soc Trans (2016) 44 (3): 856–862.
Biochem Soc Trans (2016) 44 (3): 863–868.
Biochem Soc Trans (2016) 44 (3): 869–876.
Biochem Soc Trans (2016) 44 (3): 877–882.
Biochem Soc Trans (2016) 44 (3): 883–890.
Biochem Soc Trans (2016) 44 (3): 891–897.
Biochem Soc Trans (2016) 44 (3): 898–904.
Biochem Soc Trans (2016) 44 (3): 905–915.

New Developments in Protein Structure Modelling for Biological and Clinical Research

Biochem Soc Trans (2016) 44 (3): 917–924.
Biochem Soc Trans (2016) 44 (3): 925–931.
Biochem Soc Trans (2016) 44 (3): 932–936.
Biochem Soc Trans (2016) 44 (3): 937–943.

Organelle Crosstalk in Membrane Dynamics and Cell Signalling

Biochem Soc Trans (2016) 44 (3): 945–950.

Chimeric Antigen Receptor Therapy in Haematology and Oncology: Current Successes and Challenges

Biochem Soc Trans (2016) 44 (3): 951–959.

Featured Review Article

Biochem Soc Trans (2016) 44 (3): 961–971.
  • Cover Image

    Cover Image

    issue cover
    Shining a spotlight on outer membrane protein folding. Outer membrane proteins (OMPs) [such as OmpA (green, top left)] have to navigate their way from the ribosome (bottom of image) via trigger factor (red) and SecB (turquoise), through the SecYEG translocon (red/yellow) in the inner membrane (IM). They are then chaperoned across the periplasm until they can insert and fold into their ultimate destination, the outer membrane. For further details see pp. 802–809. The figure was produced by Jim Horne.
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