The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38).
about
Survey sequencing and comparative analysis of the elephant shark (Callorhinchus milii) genomeThe sensitivity of murine spermiogenesis to miglustat is a quantitative trait: a pharmacogenetic studyThe chaperonin containing TCP1 complex (CCT/TRiC) is involved in mediating sperm-oocyte interactionLoss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesisEvolution of genes involved in gamete interaction: evidence for positive selection, duplications and losses in vertebratesPlasminogen Improves Mouse IVF by Interactions with Inner Acrosomal Membrane-Bound MMP2 and SAMP14.Ubiquitin proteasome pathway gene expression varies in rhesus monkey oocytes and embryos of different developmental potential.RAB2A: a major subacrosomal protein of bovine spermatozoa implicated in acrosomal biogenesis.The testicular and epididymal expression profile of PLCζ in mouse and human does not support its role as a sperm-borne oocyte activating factor.MMP2 and acrosin are major proteinases associated with the inner acrosomal membrane and may cooperate in sperm penetration of the zona pellucida during fertilization.Sperm proteasomes degrade sperm receptor on the egg zona pellucida during mammalian fertilization.Remodeling of the plasma membrane in preparation for sperm-egg recognition: roles of acrosomal proteins.The challenges involved in elucidating the molecular basis of sperm-egg recognition in mammals and approaches to overcome them.The Acrosomal Matrix.Sperm-egg adhesion and fusion in mammals.Proteomic analysis of bovine sperm YWHA binding partners identify proteins involved in signaling and metabolism.The mammalian zona pellucida: a matrix that mediates both gamete binding and immune recognition?The composition, protein genesis and significance of the inner acrosomal membrane of eutherian sperm.The contribution of proteomics to understanding epididymal maturation of mammalian spermatozoa.Acrosome markers of human sperm.Proteomic Characterization of Pig Sperm Anterior Head Plasma Membrane Reveals Roles of Acrosomal Proteins in ZP3 Binding.A population of CRES resides in the outer dense fibers of spermatozoa.Proteomic and functional analysis of human sperm detergent resistant membranes.First evidence of prothymosin α localization in the acrosome of mammalian male gametes.Purification and identification of sperm surface proteins and changes during epididymal maturation.Ubiquitin C-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization.Integration of the mouse sperm fertilization-related protein equatorin into the acrosome during spermatogenesis as revealed by super-resolution and immunoelectron microscopy.Improved Fertility of Diabetic Rats: Preliminary Study of Sperm ProteomiciTRAQ-based analysis of sperm proteome from normozoospermic men achieving the rescue-ICSI pregnancy after the IVF failure
P2860
Q21090196-2731CF2B-0FDB-401C-8376-5829AB4D9B47Q21245552-66F659A7-697F-44FA-8561-4321465646DBQ28586695-AEB78D6C-DA66-48E3-AB8D-BD5ED2B70C00Q28589892-72D0B082-DDBB-4735-A489-E6FD4C6EA106Q28728079-952E39A1-7905-476F-968F-7D8CEE466A57Q30277229-8BF7DF8D-23DD-4EDF-844B-4AF7BD1E9AC1Q30831977-21F99447-A82E-4B83-A1E8-22821C7319FBQ33327478-848D4F11-EC5D-4C71-ABE1-414074D51077Q34201037-128D3CFB-A8D6-4F28-9B0A-D70FC9419F4AQ34315964-2E1DD4ED-FB26-4A4B-A732-530133BACBC4Q34601181-4E6BF967-43CF-4E90-A8A4-06696F55D9ECQ35819830-18BE7C7F-8403-43BE-80E3-ED28CA571489Q36427079-5C6E1F76-5F9C-4F8B-A1DE-85AD9EC7D742Q37418556-FE8122E2-DBEE-4282-98AB-3048D7163CA7Q37428115-A228C214-851D-4307-82FF-D2F23B34542BQ37428405-46A08266-5896-4D92-9D5E-DDBCC8D0AAF3Q37775965-263B8009-AD6A-4AC9-A579-7174A954577BQ38010640-5CEA94DA-FE03-4AA0-9BE8-B9D37CB0CD35Q38025677-FA019B83-AAD3-4A53-8B1C-D2EB39274677Q38691335-4B16BE50-E5B1-48FA-9472-85448D9EE5C7Q42203769-B4CC53A3-9CF1-4A5D-A39F-4EAC249194BAQ43769306-E7F117FA-F436-4501-AA53-8A4D06425FFFQ44646010-80A638BE-5EC4-4584-9B7E-50E767B67258Q46411327-6EFB69C5-FE29-4947-8DED-30B8AFB663F3Q48677059-D2221834-026A-42A9-8C66-BB19DA2EFED2Q48786341-2421E1D5-C187-4A6F-9B12-524531E7AA10Q50482031-C0F07FB6-787B-4D5C-8525-95BBC65C22A0Q58604113-27526172-E08A-438B-BD41-35D99E4DC6E5Q58731517-4AAA65D0-378E-46FB-AAAA-22582EBFD56C
P2860
The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38).
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The extracellular protein coat ...... prominent polypeptide (IAM38).
@ast
The extracellular protein coat ...... prominent polypeptide (IAM38).
@en
type
label
The extracellular protein coat ...... prominent polypeptide (IAM38).
@ast
The extracellular protein coat ...... prominent polypeptide (IAM38).
@en
prefLabel
The extracellular protein coat ...... prominent polypeptide (IAM38).
@ast
The extracellular protein coat ...... prominent polypeptide (IAM38).
@en
P2093
P1476
The extracellular protein coat ...... prominent polypeptide (IAM38).
@en
P2093
Peter Sutovsky
Richard Oko
Young-Joo Yi
P356
10.1016/J.YDBIO.2005.11.003
P407
P577
2005-12-28T00:00:00Z