Membrane Proteins

Membrane Proteins

Donev, Rossen

Elsevier Science & Technology

01/2022

488

Dura

Inglês

9780323988957

15 a 20 dias

880

Descrição não disponível.
1. Architects of their own environment: How membrane proteins shape the Gram-negative cell envelope
Johannes Thoma and BjEURorn M. Burmann
2. Modulation of host cellular responses by gram-negative bacterial porins
Arpita Sharma, Shashi Prakash Yadav, Dwipjyoti Sarma, and Arunika Mukhopadhaya
3. Pore formation by pore forming membrane proteins towards infections
Achinta Sannigrahi and Krishnananda Chattopadhyay
4. Transmembrane ss-barrel proteins of bacteria: From structure to function
Simen Hermansen, Dirk Linke, and Jack C. Leo
5. Ribosome-membrane crosstalk: Co-translational targeting pathways of proteins across membranes in prokaryotes and eukaryotes
Krishnamoorthi Srinivasan, Aneek Banerjee, Priya Baid, Ankit Dhur, and Jayati Sengupta
6. Mechanisms of long-distance allosteric couplings in proton-binding membrane transporters
Ana-Nicoleta Bondar
7. Structures and functions of the membrane-damaging pore-forming proteins
Anish Kumar Mondal and Kausik Chattopadhyay
8. Ganglioside binding domains in proteins: Physiological and pathological mechanisms
Fodil Azzaz, Nouara Yahi, Coralie Di Scala, Henri Chahinian, and Jacques Fantini
9. Development of enhanced conformational sampling methods to probe the activation landscape of GPCRs
Ravinder Abrol, Erik Serrano, and Luis Jaimes Santiago
10. Molecular determinants of GPCR pharmacogenetics: Deconstructing the population variants in ss2-adrenergic receptor
Manali Joshi, Siddhanta V. Nikte, and Durba Sengupta
11. The role of membranes in function and dysfunction of intrinsically disordered amyloidogenic proteins
Bani Kumar Pathak, Sandip Dey, Sukanya Mozumder, and Jayati Sengupta
12. Dendritic spine membrane proteome and its alterations in autistic spectrum disorder
Ana Sofia Vall>es and Francisco J. Barrantes
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proteopolymer membrane; polymer nanodisc; beta-barrel proteins; GPCR pharmacogenomics; ganglioside; amyloidogenic proteins